Synthetic long peptides (SLP) for therapeutic vaccination against hepatitis B virus infection

ABSTRACT

The present invention relates to the fields of medicine and immunology. In particular, it relates to novel peptides that may be used in the treatment and/or prevention of a Hepatitis B viral infection and/or an Hepatitis B related disease or condition.

CROSS-REFERENCE TO RELATED APPLICATIONS

This application is the National Phase of International Patent Application No. PCT/NL2015/050390, filed Jun. 1, 2015, published on Dec. 10, 2015 as WO 2015/187009 A1, which claims priority to European Patent Application No. 14170733.1, filed Jun. 2, 2014. The contents of these applications are herein incorporated by reference in their entirety.

SEQUENCE LISTING

The instant application contains a Sequence Listing which has been submitted in ASCII format via EFS-WEB and is hereby incorporated by reference in its entirety. Said ASCII copy, created on May 8, 2017, is named 069818_2180SequenceListing.txt and is 412 KB.

FIELD OF THE INVENTION

The present invention relates to the fields of medicine and immunology. In particular, it relates to novel peptides that may be used in the treatment and/or prevention of a Hepatitis B viral infection and/or an Hepatitis B related disease or condition.

BACKGROUND OF THE INVENTION

Chronic infection with the hepatitis B virus (HBV) is a major global health problem. HBV is the prototype member of the Hepadnaviridae family, which have a strong preference for infecting liver cells (Ganem et al, 2004).

Despite the availability since three decades of an efficacious preventive vaccine for the protection against hepatitis B, an estimated two billion people have nevertheless been infected with HBV and more than 240 million currently have chronic (long-term) hepatitis B infection, with a geographical predominance in regions outside Western Europe and North America (World Health Organization, July 2013).

Transmission of the virus between people occurs by direct blood-to-blood contact or via semen or vaginal fluid of an infected person. In endemic areas, the infection occurs characteristically by perinatal transmission from mother to child. Thus, although HBV is not transmitted casually, the virus—via similar modes of entry as human immunodeficiency virus (HIV) but being at least 50 times more infectious—can be easily transmitted by perinatal, percutaneous or sexual exposure. Frequent person-to-person contact with infected individuals accordingly poses a serious risk to groups like health workers.

Infection with HBV can develop as an acute viral hepatitis, an illness that begins with general ill-health, loss of appetite, nausea, vomiting, body aches, mild fever, and dark urine, and then progresses to development of jaundice. The illness lasts for a few weeks and then gradually improves in most affected adults. A few people may have more severe liver disease (fulminant hepatic failure), and may die as a result. The infection may be entirely asymptomatic and may go unrecognized. Chronic infection with hepatitis B virus either may be asymptomatic or may be associated with a chronic inflammation of the liver (chronic hepatitis), leading to cirrhosis over a period of many years. This type of infection dramatically increases the incidence of hepatocellular carcinoma (liver cancer), also with a latency of many years.

Treatment of chronically HBV-infected individuals with antiviral drugs such as nucleoside/nucleotide analogues (e.g. Entecavir and Tenofovir) or interferon (IFN)α efficiently decreases serum viral loads. However, antiviral therapy rarely leads to a sustained virological response and drug resistance occurs (Zoulim et al., 2012). Moreover, the great majority of HBV carriers remains untreated.

Approximately 15-40% of chronic HBV carriers will develop clinically significant liver diseases in their lifetime with a high risk of death from liver cirrhosis and associated liver failure or hepatocellular carcinoma (HCC) (Lok, 2002; and Huang et al., 2011). Yearly up to one million people die worldwide due to the acute or chronic consequences of hepatitis B (Michel et al, 2001; Grimm et al, 2013). Due to the failure of antiviral drugs to eradicate infection, and consequently the need for long-term if not lifelong antiviral therapy with its drawbacks such as toxic side-effects and high costs, there is an urgent need for novel therapeutic approaches (Grimm et al., 2013).

The present invention is meant to enable efficacious therapeutic vaccination against chronic HBV infection. Therapeutic vaccination constitutes a promising strategy to treat chronic hepatitis B (Michel et al., 2011).

Next to the humoral immune response against HBV, which is predominantly involved in the protection against HBV infection by the current prophylactic vaccines (Lok, 2002), the cellular immune response is unequivocally involved in the natural resistance against HBV infection.

Perinatal transmission of HBV from mothers to neonates and infections during the first years of life result in persistent infection in more than 90% of children. By contrast, infection during adulthood clears spontaneously in more than 90% of cases and results in lifelong protective immunity (Rehermann et al., 2005).

In acute, self-limited hepatitis B virus infection, vigorous polyclonal and multispecific CD8⁺ cytotoxic T cell (CTL) and CD4⁺ T-helper (Th) cell responses to many HBV antigens are readily demonstrable in the peripheral blood (Michel et al., 2011).

These T cell responses are crucial in HBV clearance and control. Experiments in HBV-infected chimpanzees have shown the essential role of HBV-specific CD8⁺ T cells as effector cells in this process (Thimme et al., 2003). In contrast to the response in patients with resolved HBV infections, in patients with chronic hepatitis B the T cell responses are usually very weak, focused on only a few epitopes and functionally impaired (Michel et al., 2011). The goal of therapeutic vaccination is to install vigorous and robust multivalent CTL and T-helper cell responses directed to many HBV antigens, thereby pursuing viral clearance, hepatitis control and cure.

Despite the fact that great progress has been made in understanding the etiology and epidemiology of the disease, there is still a need for an effective therapeutic HBV vaccine.

DETAILED DESCRIPTION OF THE INVENTION

The inventors identified a selection of HBV antigens to be used for efficacious therapeutic vaccination. Based on HLA class I and class II binding capacities of HBV protein-derived peptides and analysis of the generation of these HLA class I binding peptides by cleavages made by the proteasome, the most immunogenic regions, covering a very high percentage of all possible T cell epitopes in the global hepatitis B patient population, have been uncovered in the HBV polymerase protein, core protein, X protein and large surface protein. These regions contain high numbers of T cell epitopes and when administered to the hepatitis B patient—either as chemically synthesized long peptide or via genetic approaches—such a vaccination is envisioned to induce a vigorous T cell response, resolving the HBV infection.

The use of relatively short peptides is highly preferred for medical purposes as these can be efficiently synthesized in vitro, which is not possible or uneconomical for native proteins larger than approximately 100, i.e. 95, 96, 97, 98, 99, 100, 101, 102, 103, 104, 105 amino acids. Chemical synthesis of peptides is routine practice and various suitable methods are known to the skilled person. Chemical synthesis of peptides also overcomes the problems associated with recombinant production of intact proteins, which is difficult to standardize and requires extensive purification and quality control measures. Peptides with a length that exceeds the length of human leukocyte antigen (HLA) class I and class II epitopes (e.g. having a length as indicated below herein) are particularly advantageous for use as vaccine component because they are large enough to be taken up by professional antigen presenting cells (APC), in particular Dendritic cell (DC), as explained in WO02/070006, and processed in the DC before cell surface presentation of the contained HLA class I-presented and HLA class II-presented epitopes takes place. Therefore, the disadvantageous induction of T cell tolerance by the systemic presentation of minimal HLA class I-presented epitopes on non-antigen presenting cells (as shown in Toes et al., 1996a, and Toes et al., 1996b), is prevented by the application of peptides exceeding the length of human leukocyte antigen (HLA) class I and class II epitopes (as shown in Zwaveling et al., 2002).

The present invention relates to novel peptides of about 15 to about 100 amino acids in length, also denominated herein as long peptides, that each exceed the length of human leukocyte antigen (HLA) class I and class II presented epitopes and that induce a combined CD4⁺ and CD8⁺ T cell response that is therapeutically successful and inducing cure in a high percentage of patients. Preferably, the long peptides of the invention are synthetic peptides, denominated herein as synthetic long peptides (SLPs). As compared to vaccination with the peptides of the present invention, therapeutic vaccination with full length HBV proteins is likely to be less potent (Rosalia et al., 2013). From the viewpoint of manufacture and administration of peptides to patients, immunization with the complete set of overlapping long peptides or SLPs spanning the full length HBV polymerase, HBV core protein, HBV X protein and HBV large surface protein is not feasible. To narrow the number of peptides in a vaccine, it is needed to incorporate the most immunogenic SLPs that are recognized by the highest percentage of patients. The present invention provides for peptides and peptide vaccines to meet this need. Using a stepwise sophisticated selection procedure based on bioinformatics analyses that are experimentally underpinned, the long peptide and/or SLP sequences with the highest coverage of HLA class I-restricted cytotoxic T lymphocyte epitopes and HLA class II-restricted T helper epitopes were identified. The selections as described herein identify the long peptide and/or SLP sequences that incorporate HBV-derived T cell epitopes that are presented on all predominantly expressed HLA class I and class II alleles. By covering the vast majority of worldwide expressed HLA haplotypes (Bui et al., 2006), the long peptide and/or SLP vaccine composition can be used in all HBV infected individuals. The present invention describes the identification and selection of HBV-derived long peptides, preferably SLPs, that are highly immunogenic and capable of inducing a potent combined HBV-directed CD4⁺ T helper and CD8⁺ cytotoxic T cell response, when administered as a vaccine composition to patients. Such highly immunogenic long peptides from HBV have not been disclosed in the prior art. The HBV-derived long peptides of the invention were identified based on a putative immunogenicity score developed and validated by the inventors and as disclosed herein. The putative immunogenicity is quantified herein using the T cell Regional Immunogenicity Assessment (TRIA) score. The TRIA score is based on the cumulative Class I-BCI score of said peptide, which is indicative for their immunogenic CTL activating capacity, and the cumulative Class II-B score of said peptide, which is indicative for their immunogenic Th-cell activating capacity. Calculation of the cumulative Class I-BCI score and the cumulative Class II-B score is described in detail herein in the Examples section. The TRIA score is calculated as the sum of the cumulative Class I-BCI score and the cumulative Class II-B score. A strong correlation was found between this TRIA score and the T cell responses found in PBMC of HBV-immune donors. Therefore, the TRIA score enables the selection of optimal immunogenic long peptides.

In a first aspect, the present invention provides a peptide derived from an HBV protein. Preferably the peptide of the invention comprises or consists of a peptide selected from the group consisting of SEQ ID NO: 51-79, 1142-1145 and 1468-1471, more preferably the peptide of the invention comprises or consist of a peptide selected from the group consisting of SEQ ID NO: 51, 55, 60, 63, 64, 68, 71, 74, 75, 76, 77, 1142 and 1469, more preferably selected from the group consisting of SEQ ID NO: 51, 55, 60, 63, 64, 68, 71, 74, 75, 77, 1142 and 1469, even more preferably selected from the group consisting of SEQ ID NO: 55, 60, 63, 64, 68, 71, 74, 75, 76, 77 and 1469, even more preferably selected from the group consisting of SEQ ID NO: 55, 60, 63, 64, 68, 71, 74, 75, 77 and 1469, even more preferably selected from the group consisting of SEQ ID NO: 60, 63, 71, 74, 75 and 1469, most preferably selected from the group of SEQ ID NO: 75, 1469 and 63. Further preferred is a peptide of the invention that comprises or consists of a peptide selected from the group consisting of SEQ ID NO: 51, 60, 63, 64, 68, 71, 74-77. Also preferred is a peptide of the invention that comprises or consists of a peptide selected from the group consisting of SEQ ID NO: 63, 71 and 75. Preferably, the peptide of the invention comprises at least about 70 predicted T-cell epitopes. More preferably, the peptide of the invention comprises at least about 70 predicted T-cell epitopes and at least about 3 proteasomal cleavage sites. Preferably, the peptide if the invention comprises at least about 70 predicted HLA class I-restricted CD8⁺ cytotoxic T-cell epitopes, at least about 1 predicted HLA class II-restricted CD4⁺ T-helper epitope. More preferably, the peptide if the invention comprises at least about 70 predicted HLA class I-restricted CD8⁺ cytotoxic T-cell epitopes, at least about 1 predicted HLA class II-restricted CD4⁺ T-helper epitope and at least about 3 proteasomal cleavage sites. HLA class I-restricted CD8⁺ cytotoxic T-cell epitope is also denominated herein as CTL epitope and HLA class II-restricted CD4⁺ T-helper epitope is also denominated herein as Th-cell epitope. Preferably, the peptide of the invention comprises at least about 70 predicted CTL epitopes, at least about 15 predicted Th-cell epitopes. More preferably, the peptide of the invention comprises at least about 70 predicted CTL epitopes, at least about 15 predicted Th-cell epitopes and at least about 3 proteasomal cleavage sites. Preferably, the peptide of the invention comprises at least about 95 predicted CTL epitopes, at least about 25 predicted Th-cell epitopes. More preferably, the peptide of the invention comprises at least about 95 predicted CTL epitopes, at least about 25 predicted Th-cell epitopes and at least about 3 proteasomal cleavage sites. Preferably, the peptide of the invention comprises at least about 125 predicted CTL epitopes, at least about 50 predicted Th-cell epitopes. More preferably, a peptide of the invention comprises at least about 125 predicted CTL epitopes, at least about 50 predicted Th-cell epitopes and at least about 3 proteasomal cleavage sites. Preferably, a peptide of the invention has a TRIA score of at least about 6300, at least about 8000, at least about 9000, at least about 10000, or preferably at least about 14000.

A peptide of the invention can advantageously be used in the prevention and/or treatment of an HBV related disease or condition in a subject, preferably a mammal, more preferably a human. Preferably, the peptide of the invention comprises or consists of an amino acid sequence, preferably a contiguous amino acid sequence, of any of the proteins selected from the group consisting of HBV protein polymerase, HBV core protein, HBV X-protein and HBV large surface protein. Preferably, said peptide comprises or consists of a peptide selected from the group consisting of SEQ ID NO: 51-79, 1142-1145 and 1468-1471. A peptide of this group is characterized in that it has a TRIA score of at least 6300, indicating the high immunogenic capacity for CD4+ and CD8+ T cell activation. Furthermore, a peptide of this group is characterized in that it comprises at least 70 predicted HLA class I-restricted CD8⁺ cytotoxic T-cell epitopes, at least 1 predicted HLA class II-restricted CD4⁺ T-helper epitope. Preferably, a peptide of this group comprises at least 3 proteasomal cleavage sites.

More preferably, the peptide of the invention comprises or consists of a peptide selected from the group consisting of SEQ ID NO: 51-53, 55-57, 60-66, 68-78, 1142-1145 and 1468-1471. A peptide of this group is characterized in that it has a TRIA score of at least 8000.

More preferably, the peptide of the invention comprises or consists of a peptide selected from the group consisting of SEQ ID NO: 51-53, 55-57, 60-66, 68, 69, 71-79, 1142-1145 and 1468-1471. A peptide of this group is characterized in that it comprises at least 70 predicted CTL epitopes, at least 15 predicted Th-cell epitopes. Preferably, a peptide of this group comprises at least 3 proteasomal cleavage sites. Preferably, the peptide of the invention comprises or consists of a peptide selected from the group consisting of SEQ ID NO: 51-53, 55, 57, 60, 63, 64, 66, 68, 71, 72, 74-78, 1142, 1145, 1468-1471.

More preferably, the peptide of the invention comprises or consists of a peptide selected from the group consisting of SEQ ID NO: 53, 55-57, 60-66, 68, 69, 71, 73-78, 1142-1145, 1468-1471. A peptide of this group is characterized in that it has a TRIA score of at least 9000.

Even more preferably, the peptide of the invention is a peptide that comprises or consists of a peptide selected from the group consisting of SEQ ID NO: 55-57, 60-65, 68, 69, 71, 74, 75, 77, 78, 1142-1145, 1468, 1469 and 1471. A peptide of this group is characterized in that it has a TRIA score of at least 10000.

Even more preferably, the peptide of the invention comprises or consists of a peptide selected from the group consisting of SEQ ID NO: 52, 53, 55, 57, 60, 61, 63, 64, 68, 69, 71, 72, 75, 77, 78, 1142-1145, 1468, 1469 and 1471. A peptide of this group is characterized in that it comprises at least 95 predicted CTL epitopes, at least 25 predicted Th-cell epitopes. Preferably, a peptide of this group comprises at least 3 proteasomal cleavage sites. Preferably, the peptide of the invention comprises or consists of a peptide selected from the group consisting of SEQ ID NO: 55, 60, 63, 64, 68, 71, 75, 77, 1142, 1469.

Most preferably, the peptide of the invention comprises or consists of a peptide selected from the group consisting of SEQ ID NO: 63, 75, 1143-1145, 1468 and 1469. A peptide of this group is characterized in that it has a TRIA score of at least 14000. Furthermore, a peptide of this group is characterized in that it comprises at least 125 predicted CTL epitopes, at least 50 predicted Th-cell epitopes. Preferably, a peptide of this group comprises at least 3 proteasomal cleavage sites.

A “T-cell epitope” is defined herein as a linear fragment of a polypeptide antigen, which is recognized and bound by a T-cell receptor, preferably a human T-cell receptor, after being made accessible to a T-cell receptor by intracellular proteolytic processing of the polypeptide antigen and subsequent presentation by an HLA class I or HLA class II molecule on the cell surface of an antigen-presenting cell. A “predicted T-cell epitope” is to be understood herein as a linear fragment of a polypeptide antigen for which liberation from the source protein or peptide by proteolytic cleavage and T-cell receptor recognition and/or binding has been predicted using bioinformatics analyses based on algorithms that predict HLA class I and II peptide binding and C-terminal generation by the proteasome of all possible HLA class I binding peptides (with a length of a HLA class I ligand; 8-12 aa) contained in the HBV proteins. A “confirmed T-cell epitope” is to be understood herein as a linear fragment of a polypeptide antigen for which liberation from the source protein or source polypeptide by proteolytic cleavage and T-cell receptor recognition and/or binding, and more preferably CD4⁺ or CD8⁺ T cell activation capability, have been established experimentally as disclosed herein. A “linear fragment” is understood herein to be a contiguous amino acid sequence of a polypeptide antigen, said polypeptide antigen preferably being an HBV protein, more preferably a protein selected from the group consisting of HBV protein polymerase, HBV core protein, HBV X-protein and HBV large surface protein. An identical linear fragment of a polypeptide antigen showing binding affinity to a second or further type of HLA class I or HLA class II molecule is to be understood herein as a second or further T-cell epitope. In other words, a specific linear fragment of a polypeptide antigen being capable to bind to two types of HLA molecules is understood herein to be two separate or distinct T-cell epitopes, and is scored twice within the cumulative BCI Class I- and/or Class II-B score. A T-cell epitope typically comprises or consists of at least 8 amino acids and up to 20 or (exceptionally) even more amino acids. A T-cell epitope can be an HLA class I-restricted CD8⁺ cytotoxic T cell (CTL) epitope or an HLA class II-restricted CD4⁺ T-helper (Th-)cell epitope. HLA class I restricted epitopes (also referred to as CTL epitopes) are typically presented via the classical proteasome dependent HLA class I processing route, whereas HLA class-II molecules are typically loaded with linear fragments in the late endosomal compartment. Preferably, a peptide according to the invention comprises T-cell epitopes that are selected from the group consisting of SEQ ID NO: 80-276, 278-314, 316-429, 432-483, 486-545, 548-636, 638-1140, and 1146-1466 (see Tables 4-7). A preferred peptide according to the invention comprises at least 70, 71, 72, 73, 74, 75, 79, 80, 85, 90, 95, 100, 105, 110, 115, 120, 125, 130, 135, 140, 145, 150, 155, 160, 165, 170, 175, 180, 185, 190, 195, 200, 205, 210, 215, 220, 225 or from about 230 to about 233 predicted T-cell epitopes from HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein. A more preferred peptide according to the invention comprises at least 95, 96, 97, 98, 100, 105, 110, 115, 120, 125, 130, 135, 140, 145, 150, 155, 160, 165, 170, 175, 180, 185, 190, 195, 200, 205, 210, 215, 220, 225 or from about 230 to about 233 predicted T-cell epitopes from HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein. An even more preferred peptide according to the invention comprises at least 70, 71, 72, 73, 74, 75, 79, 80, 85, 90, 95, 100, 105, 110, 115, 120, 125, 130, 135, 140, 145, 150, 155, 160, 165, 170, 175, 180, 185, 190, 195, 200, 205, 210, 215, 220, 225 or from about 230 to about 233 predicted T-cell epitopes selected from the group consisting of SEQ ID NO: 80-276, 278-314, 316-429, 432-483, 486-545, 548-636, 638-1140, and 1146-1466. An even more preferred peptide according to the invention comprises at least 95, 96, 97, 98, 100, 105, 110, 115, 120, 125, 130, 135, 140, 145, 150, 155, 160, 165, 170, 175, 180, 185, 190, 195, 200, 205, 210, 215, 220, 225 or from about 230 to about 233 predicted T-cell epitopes selected from the group consisting of SEQ ID NO: 80-276, 278-314, 316-429, 432-483, 486-545, 548-636, 638-1140, and 1146-1466. Preferably, the predicted T-cell epitopes of the present invention are confirmed experimentally as disclosed herein. A preferred peptide according to the invention comprises at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65 or 70 confirmed T-cell epitopes from HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein. A more preferred peptide according to the invention comprises at least 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90 or 95 confirmed T-cell epitopes from HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein. An even more preferred peptide according to the invention comprises at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65 or 70 confirmed T-cell epitopes selected from the group consisting of SEQ ID NO: 80-276, 278-314, 316-429, 432-483, 486-545, 548-636, 638-1140, and 1146-1466. An even more preferred peptide according to the invention comprises at least 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90 or 95 confirmed T-cell epitopes selected from the group consisting of SEQ ID NO: 80-276, 278-314, 316-429, 432-483, 486-545, 548-636, 638-1140, and 1146-1466.

A “proteasomal cleavage site” is understood herein as a site in a protein or polypeptide that is cleaved by the proteasome, preferably a human proteasome/proteasome naturally present in a human cell. A specific proteasomal cleavage site liberating the C-terminus of the epitope is preferably present exactly after the C-terminus of the epitope amino acid sequence, in order to allow the epitope's C-terminal residue to be liberated from the larger peptide and to be presented by the HLA class I molecule. The first important event that defines an HLA class I-restricted CD8⁺ cytotoxic T-cell (CTL) epitope is the release of the epitope (or the epitope-precursor) from its flanking protein regions through enzymatic cleavage by cytosolic peptidases.

The multicatalytic proteasome is the primary enzyme complex required for the generation of the exact C-terminus of the vast majority of CTL epitopes (Rock et al., 2004). Proteasomes are multicatalytic enzyme complexes abundantly present intracellularly and are considered responsible for the generation of the C terminus of the vast majority of CTL epitopes (Craiu et al, 1997; Stoltze et al., 1998; Mo et al., 1999). The generation of the amino-terminus of a CTL epitope, on the other hand, is much more flexible because several amino-terminal exo-peptidases (like ERAP1, puromycin sensitive aminopeptidase, bleomycin hydrolase and others) reside in the cytosol and endoplasmic reticulum and these trimming enzymes have the capacity to shorten an N-terminal elongated epitope-precursor to its precise length. In contrast, C-terminal trimming has not been reported. Therefore the identification of the proteasome-mediated cleavage sites in a protein or in a polypeptide, like a peptide of the invention, can be used as an important identifier of almost every CTL epitope, because the proteasomal cleavages determine and enable C-terminal epitope generation (Kessler et al., 2001; Kessler and Melief, 2007). The assessment of proteasomal cleavage sites in the HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein identifies the C-termini of intracellularly produced HBV peptide fragments, specifically for HLA class I presented peptide fragments. Length requirements are much less strict for loading of HLA class II with peptide fragments. Therefore, precise enzymatic generation of the HLA class II binding peptide fragment is not needed. These T-cell epitope requirements have been used in the present invention to localize and design long peptides derived from the full length sequences of an HBV protein which comprises preferred CD8⁺ cytotoxic T cell (CTL) and CD4⁺ T-helper (Th-)cell epitopes and/or combinations thereof and are thus highly immunogenic and therefore suitable peptides for synthesis and (therapeutic) vaccination purposes.

Proteasome mediated proteolytic cleavages can be predicted in silico using a prediction algorithm. Cleavage as performed by the proteasome can be verified in a proteasome mediated cleavage assay as disclosed herein, which measures the C-terminal liberation of the epitope from its flanking regions (Kessler et al., 2001; Kessler and Melief, 2007). A cell free proteasome cleavage assay identifying and quantitatively measuring the amino acid (aa) positions and the abundancy of cleavages by the proteasome in a polypeptide can be used to determine which peptides are generated from the source protein (or source polypeptide), thereby establishing the peptide pool available for epitope generation. The cell free proteasome cleavage assay involves the co-incubation of a polypeptide (preferably having a length of 28-40 aa, more preferably having a length of 30-39 aa) with a preparation of purified proteasomes in an appropriate buffer solution. Two main forms of proteasomes exist, the immunoproteasomes, which are mainly expressed in professional antigen presenting cells, like e.g. Dendritic Cells, and the constitutive proteasomes, which are expressed mainly in other cell types. These types contain variant catalytic subunits with slightly different catalytic activity. Although most epitopes are liberated by both types of proteasomes, sometimes differential epitope generation occurs dependent on proteasome type (Morel et al., 2000; Chapiro et al., 2006). Accordingly, proteasome-mediated cleavage assays may be performed separately with these two proteasome types. Preferably, a constitutive 20S-proteasome or immune 20S-proteasome is used as disclosed herein. The reaction mixture comprising the peptides to be cleaved and either of the two proteasome types (purified proteasome preparations) is incubated at 37° C. and samples are drawn at 1 h, 3 h, 6 h and 24 h time points as detailed in the Examples herein. Subsequently, generated peptide cleavage fragments and the remaining source polypeptide are identified and quantified by mass spectrometry (Kessler et al., 2001). This assay reveals both the positions in the polypeptide (and thus in the source protein) where the proteasome cleaves and the cleavage efficiency (abundancy) at these positions. A cleavage site can be confirmed by detection of fragments containing as COOH terminus the residue NH2-terminal from the cleavage site together with the (possible) complementary fragment(s), as calculated from the intensities of the fragment peaks in the mass spectra (preferably present for >1%, more preferably present for ≥7%, at 24 h incubation), in both the digestion with constitutive proteasomes and the digestion with immunoproteasomes. Preferably, a peptide of the invention comprises at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20 or more, preferably at least 3, proteasomal cleavage site as defined herein. More preferably, a peptide of the invention comprises at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20 or more, preferably at least 3, proteasomal cleavage site as assessed and verified in a proteasomal cleavage assay as described above.

As indicated above, examples of T-cell epitopes are HLA class I-restricted CD8⁺ cytotoxic T cell (CTL) epitopes and HLA class II-restricted CD4⁺ T-helper (Th-)cell epitopes. A “CTL epitope” is understood herein as a linear fragment of a polypeptide antigen that is liberated from the source protein by proteasome mediated proteolytic cleavage and subsequently presented by an HLA class I molecule on the cell surface of an antigen presenting cell (APC), preferably a human antigen presenting cell. A “predicted CTL epitope” is understood herein as a linear fragment of a polypeptide antigen for which liberation from its source protein by proteolytic cleavages and HLA class I molecule binding have been predicted using bioinformatics analyses based on algorithms that predict HLA class I peptide binding and C-terminal generation by the proteasome of all HLA class I binding short peptides (with a length of a CTL epitope; 8-12 aa) contained in the HBV proteins. Preferably, a predicted CTL epitope of the present invention is confirmed experimentally as disclosed herein. A CTL epitope of the invention is preferably capable of activating a CD8⁺ T cell response. A “confirmed CTL epitope” is understood herein as a linear fragment of a polypeptide antigen for which liberation by proteolytic cleavages and HLA class I molecule binding, more preferably CD8⁺ T cell activation, have been established experimentally as disclosed herein. A CTL epitope of the invention is preferably capable of activating a CD8⁺ T cell response. A CTL epitope typically comprises at least 8 up to 12, or exceptionally up to 13 or 14 amino acids. Preferably a CTL epitope consists of 8-14 amino acids, i.e. has a length of at least 8 up to 14 amino acids.

A CTL epitope is defined by two important intracellular events being (i) proteasome mediated proteolytic cleavage and (ii) binding to an HLA class I molecule, which takes place in the endoplasmic reticulum (ER). The stronger a linear peptide fragment binds and the slower the off-rate, the more likely that this linear peptide fragment will become a cell surface presented immunogenic CTL epitope (Van der Burg et al., 1996). Analysis of proteasome mediated proteolytic cleavages can be performed as indicated above. Preferably, specific binding to an HLA class I molecule is predicted using an in silico prediction algorithm and established by using an HLA class I peptide binding assay as known by the person skilled in the art (Kessler and Melief, 2007; Kessler et al., 2003). Preferably, the HLA class I-restricted epitope in a long peptide according to the invention is predicted to be generated at its C-terminus by the proteasome and preferably has a predicted high affinity binding capacity for the HLA class I molecule using an assay as described in van der Burg et al., 1995 and Kessler et al., 2003; e.g. IC₅₀≤about 5 μM may be considered high affinity binding, about 5 μM<IC₅₀≤about 15 μM may be considered intermediate affinity binding, about 15 μM<IC₅₀≤100 μM may be considered low affinity binding and IC₅₀>about 100 μM may be considered as no binding. To measure class I binding affinity of a peptide or fragments thereof, various HLA class I binding assays are available. The assays can be divided into cell-free assays (using soluble HLA) versus cellular assays (using HLA class I molecules on the cell surface), and competitive assays (resulting in semi-quantitative data) versus assays that do not use a labeled reference peptide and are therefore quantitative (Kessler and Melief, 2007; Viatte et al., 2006). The assays have in common that the HLA class I peptide binding affinity is reliably assessed.

The actual presentation of a CTL epitope on the cell surface, i.e. the net result of both proteasomal cleavage, possible other proteolytic events like N-terminal trimming, and binding and presentation by an HLA class I molecule, which events together define a CTL epitope as indicated above, can be demonstrated by a biochemical approach or by a functional approach using cytotoxic T cells with a T-cell receptor specific for the epitope and HLA class I molecule (geno)type, as known by the person skilled in the art (Kessler and Melief, 2007).

The biochemical approach involves the biochemical purification of HLA-epitope complexes from cells expressing the HBV antigen of the invention together with the presenting HLA class I molecule (geno)type, followed by the mass spectrometric search for the epitope in the eluted HLA class I-bound CTL receptor ligands as known by the person skilled in the art (Schirle et al., 2000; Schirle et al., 2001).

The functional approach involves a CTL line or clone that is specifically recognizing the HLA-epitope, which is used as a tool to demonstrate the natural processing and actual presentation of the epitope by HLA class I molecules. In this methodology, using a CTL induction assay as known in the art, either the synthetically generated minimal (i.e. exact length) epitope or the peptide sequence of interest encompassing the epitope, for instance a peptide, long peptides and/or SLP as defined herein, is used to stimulate and select HLA-epitope-specific cytotoxic T cells. To that end, briefly, a multivalent CD8⁺ T cell population, or a multivalent mixed CD8⁺ and CD4⁺ T cell population, is stimulated with autologous target cells of which the HLA class I molecules on the cell surface are either exogenously loaded with the precise synthetic epitope or endogenously loaded with intracellularly generated CTL epitopes derived from the exogenously loaded long peptide of the invention after its uptake by the antigen presenting target cells. In case the autologous target cells are loaded with a peptide, e.g. the synthetic long peptide of the invention, or fragments thereof, encompassing the epitope, the epitope is generated after cellular uptake of the peptide and its intracellular processing by the proteasome together with other N-terminal trimming peptidases. Subsequently, using a T cell recognition assay, the HLA-epitope-specific CTL is used to demonstrate the intracellular generation and natural presentation of the epitope of the invention by HLA class I molecules on the surface of HBV-infected cells. Specific recognition of an HLA class I restricted epitope by a CTL demonstrates the cell surface expression of the epitope and reveals its immunogenicity, i.e. the presence of epitope-specific T cells in the (T-cell receptor) repertoire of a selected donor. Preferably, the CD8⁺ T cell activating capability has been demonstrated ex vivo and/or in vivo, in T cells from human healthy control individuals or even more preferably in T cells from a human patient with an HBV related disease or condition and/or from a healthy control. The activation is preferably assessed ex vivo or in vivo, more preferably in a human patient with an HBV related disease. A CTL epitope for which liberation by proteolytic cleavage and HLA class I molecules presentation, or preferably CD8+ T cell activating capability, has been demonstrated experimentally is denominated herein as a confirmed CTL epitope.

A peptide of the invention preferably comprises at least 70, 71, 72, 73, 74, 75, 79, 80, 85, 90, 95, 100, 105, 110, 115, 120, 125, 130, 135, 140, 145, 150, 155, 160, 165, 170, 175, 180, 185, 190, 195, 200, 205, 210, 215, 220, 225, 230 and to up to 233 predicted CTL epitopes as defined herein. Preferably, a peptide of the invention comprises at least 70, 71, 72, 73, 74, 75, 79, 80, 85, 90, 95, 100, 105, 110, 115, 120, 125, 130, 135, 140, 145, 150, 155, 160, 165, 170, 175, 180, 185, 190, 195, 200, 205, 210, 215, 220, 225, 230 and to up to 233 predicted CTL epitopes as defined herein. Preferably, a peptide according to the invention comprises at least 70, 71, 72, 73, 74, 75, 79, 80, 85, 90, 95, 100, 105, 110, 115, 120, 125, 130, 135, 140, 145, 150, 155, 160, 165, 170, 175, 180, 185, 190, 195, 200, 205, 210, 215, 220, 225, 230 and to up to 233 predicted CTL epitopes from the HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein. More preferably a peptide according to the invention comprises at least 70, 71, 72, 73, 74, 75, 79, 80, 85, 90, 95, 100, 105, 110, 115, 120, 125, 130, 135, 140, 145, 150, 155, 160, 165, 170, 175, 180, 185, 190, 195, 200, 205, 210, 215, 220, 225, 230 and to up to 233 predicted CTL epitopes from the HBV core protein, HBV polymerase, HBV X protein or HBV large surface protein. Even more preferably, a peptide according to the invention comprises or consists of a contiguous amino acid sequence of any of the proteins selected from the group consisting of HBV core protein, HBV polymerase, HBV X protein and HBV large surface protein, wherein said contiguous amino acid sequence comprises at least 70, 71, 72, 73, 74, 75, 79, 80, 85, 90, 95, 100, 105, 110, 115, 120, 125, 130, 135, 140, 145, 150, 155, 160, 165, 170, 175, 180, 185, 190, 195, 200, 205, 210, 215, 220, 225, 230 and to up to 233 predicted CTL epitopes. Preferably, a peptide according to the invention comprises at least 70, 71, 72, 73, 74, 75, 79, 80, 85, 90, 95, 100, 105, 110, 115, 120, 125, 130, 135, 140, 145, 150, 155, 160, 165, 170, 175, 180, 185, 190, 195, 200, 205, 210, 215, 220, 225, 230 and to up to 233 CTL predicted epitopes selected from the group consisting of SEQ ID NO: 80-276, 278-314, 316-429, 432-483, 486-545, 548-636, 638-685; 846-923, 959-1090, and 1146-1395 (see Tables 4a, 5a, 6a and 7a). Even more preferably, a peptide of the invention preferably comprises at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 15, 20, 25, 30, 40, 50, 60, 70, or preferably at least 95 confirmed CTL epitopes as defined herein and verified using a biochemical or functional assay as described above. Most preferred is a peptide of the invention that comprises at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65 or 70 or preferably at least 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90 or 95 confirmed CTL epitopes as defined herein and verified using a functional assay as described above. Preferably, a peptide of the invention comprises at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65 or 70 or preferably at least 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90 or 95 confirmed CTL epitopes selected from the group consisting of SEQ ID NO: 80-276, 278-314, 316-429, 432-483, 486-545, 548-636, 638-685; 846-923, 959-1090, and 1146-1395.

A “Th-cell epitope” is understood herein to be a linear peptide fragment that is recognized by an HLA class II molecule. A “predicted Th-cell epitope” is understood herein as a linear fragment of a polypeptide antigen for which HLA class II molecule recognition has been predicted using sophisticated bioinformatics analyses that are experimentally underpinned. Preferably, a predicted Th-cell epitope of the present invention is confirmed experimentally as disclosed herein. A Th-cell epitope of the invention is preferably capable of inducing a CD4⁺ T cell response. A “confirmed Th-cell epitope” is understood herein as a linear fragment of a polypeptide antigen for which HLA class II molecule recognition has been established experimentally as known by the person skilled in the art and further detailed herein.

An HLA class II-restricted CD4⁺ T-helper cell (Th-cell) epitope typically comprises 15 up to 20, or exceptionally even more, amino acids. Preferably, an HLA class II-restricted T-helper cell epitope comprises or 10-20 or 10-15 amino acids. Specific recognition of a predicted HBV-derived Th-cell epitope can be tested and/or verified in a Th-cell induction assay. To this end the peptide or fragment thereof, long peptide and/or SLP sequence of interest comprising the predicted Th-cell epitope is exogenously loaded on the surface of target cells and subsequently these peptide-loaded target cells are co-incubated with a multivalent autologous T helper cell population. After several rounds of stimulation, epitope-specific T helper cells can be selected and can be back-tested for the recognition of the T helper cell epitope contained in the peptide or SLP thereby proving its natural cell surface presentation. Preferably, an HLA class II-restricted CD4⁺ T-helper cell epitope comprised in a peptide according to the invention is capable of inducing or activating a CD4⁺ T-helper cell in a human patient with an HBV related disease or condition. The induction or activation is preferably assessed ex vivo or in vivo, more preferably in a human patient with an HBV related disease. Most preferably, the HLA class II-restricted epitope is capable of activating a CD4⁺ T-helper memory and/or CD4⁺ T-helper effector response, i.e. activation of a CD45RO-positive CD4⁺ T-helper cell. This will lead, by virtue of the ‘license to kill’ signal through CD40-triggering of DC (Lanzavecchia, 1998) to a more robust CD8⁺ effector and memory cytotoxic T cell response. In another setting the activated CD4⁺ T-helper cells may activate non-HLA restricted killer cells of the immune system. A Th-cell epitope for which recognition by an HLA class II molecule, or preferably CD4+ activating capability, has been demonstrated experimentally is denominated herein as a confirmed Th-cell epitope.

Preferably, a peptide according to the invention comprises at least one predicted Th-cell epitope from HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein. Preferably, a peptide of the invention comprises at least 1, 2, 3, 4, 5, 6, 8, 7, 8, 9, 10 or preferably at least 15 predicted Th-cell epitope(s) as defined herein. Preferably, a peptide according to the invention comprises at least 1, 2, 3, 4, 5, 6, 8, 7, 8, 9, 10, or preferably at least 15 predicted Th-cell epitope(s) from the HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein. Even more preferably, a peptide according to the invention comprises or consists of a contiguous amino acid sequence of any of the proteins selected from the group consisting of HBV core protein, HBV polymerase, HBV X protein and HBV large surface protein, wherein said contiguous amino acid sequence comprises at least 1, 2, 3, 4, 5, 6, 8, 7, 8, 9, 10, or preferably at least 15 predicted Th-cell epitope(s). Preferably, a peptide according to the invention comprises at least 1, 2, 3, 4, 5, 6, 8, 7, 8, 9, 10, or preferably at least 15 predicted Th-cell epitope(s) selected from the group consisting of SEQ ID NO: 686-845; 924-958, 1091-1140, and 1396-1466 (see Tables 4b, 5b, 6b, and 7b). More preferably, a peptide of the invention comprises at least 1, 2, 3, 4, 5, 6, 8, 7, 8, 9, 10, or preferably at least 15 confirmed Th-cell epitope(s) as defined herein. Even more preferably, a peptide of the invention comprises at least 1, 2, 3, 4, 5, 6, 8, 7, 8, 9, 10, or preferably at least 15 confirmed Th-cell epitope(s) as defined herein and verified using an T helper cell induction assay as described above. Preferably, a peptide of the invention comprises at least 1, 2, 3, 4, 5, 6, 8, 7, 8, 9, 10, or preferably at least 15 confirmed Th-cell epitope selected from the group consisting of SEQ ID NO: 686-845; 924-958, 1091-1140, and 1396-1466.

Preferably, a peptide according to the invention comprises both at least 70 predicted CTL epitopes and at least one predicted Th-cell epitope from the HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein. More preferably, a peptide according to the invention is a peptide derived from the HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein, preferably is a fragment of the HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein, that comprises at least 70 predicted CTL epitopes, at least one predicted Th-cell epitope and at least 3 proteasomal cleavage sites. The presence of at least 3 proteasomal cleavage sites, at least 70 predicted CTL epitopes and at least 1 Th epitope within a single peptide according to the invention, being a continuous amino acids fragment of an antigen protein of interest, has been observed to be particularly advantageous due to synergy between the Th response and the CTL response in mounting and maintaining an effective CD8⁺ cytotoxic T cell response. Several published studies have demonstrated that CD4⁺ T-helper cells upon interaction with HLA class II epitope presenting dendritic cells (DC) upregulate CD40 ligand. The interaction of the Th-cell by its CD40 ligand with the CD40 molecule on the DC leads to activation of the DC. Activated DCs display upregulated costimulatory molecules and secrete CTL-promoting cytokines. This allows both a more robust CD8⁺ CTL response induced by such an activated DC that presents HLA class I restricted epitopes and a much more robust CTL memory response (Ridge et al., 1998; Schoenberger et al., 1998; Sun et al., 2004). The need for CD40 expression on DC for robust CD8⁺ CTL responses following vaccination with synthetic long peptides (length of 35 aa.) has been demonstrated in Zwaveling et al. (2002).

Accordingly, a preferred peptide according to the invention comprises at least 70 predicted CTL epitopes and at least one predicted Th-cell epitope; preferably at least 70 predicted CTL epitopes selected from the group consisting of SEQ ID NO: 80-276, 278-314, 316-429, 432-483, 486-545, 548-636, 638-685; 846-923, 959-1090, and 1146-1395 and at least one predicted Th-cell epitope selected from the group consisting of SEQ ID NO: 686-845; 924-958, 1091-1140, and 1396-1466. A more preferred peptide according to the invention comprises at least 70 predicted CTL epitopes and at least 15 predicted Th-cell epitopes; preferably at least 70 predicted CTL epitopes selected from the group consisting of SEQ ID NO: 80-276, 278-314, 316-429, 432-483, 486-545, 548-636, 638-685; 846-923, 959-1090, and 1146-1395 and at least 15 predicted Th-cell epitopes selected from the group consisting of SEQ ID NO: 686-845; 924-95, 1091-1140, and 1396-1466. More preferably, a peptide according to the invention comprises at least 71, 72, 73, 74, 75, 80, 85, 90, 95, 100, 105, 110, 115, 120, 125, 130, 135, 140, 145, 150, 155, 160, 165, 170 up to 175 predicted CTL epitopes selected from the group consisting of SEQ ID NO: 80-276, 278-314, 316-429, 432-483, 486-545, 548-636, 638-685; 846-923, 959-1090, and 1146-1395 and at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56, 57, 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95 up to 96 predicted Th-cell epitopes selected from the group consisting of SEQ ID NO: 686-845; 924-958, 1091-1140, and 1396-1466. Even more preferably, a peptide according to the invention comprises at least 95, 100, 105, 110, 115, 120, 125, 130, 135, 140, 145, 150, 155, 160, 165, 170 up to 175 predicted CTL epitopes selected from the group consisting of SEQ ID NO: 80-276, 278-314, 316-429, 432-483, 486-545, 548-636, 638-685; 846-923, 959-1090, and 1146-1395 and at least 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44, 45, 46, 47, 48, 49, 50, 51, 52, 53, 54, 55, 56, 57, 58, 59, 60, 61, 62, 63, 64, 65, 66, 67, 68, 69, 70, 71, 72, 73, 74, 75, 76, 77, 78, 79, 80, 81, 82, 83, 84, 85, 86, 87, 88, 89, 90, 91, 92, 93, 94, 95 up to 96 predicted Th-cell epitopes selected from the group consisting of SEQ ID NO: 686-845; 924-958, 1091-1140, and 1396-1466. Preferably, a peptide according to the invention comprises at least 95 predicted CTL epitopes as defined herein and at least 25 predicted Th-cell epitopes as defined herein.

More preferably, a preferred peptide according to the invention comprises at least 5 confirmed CTL epitopes and at least one confirmed Th-cell epitope; preferably at least 5 confirmed CTL epitopes selected from the group consisting of SEQ ID NO: 80-276, 278-314, 316-429, 432-483, 486-545, 548-636, 638-685; 846-923, 959-1090, and 1146-1395 and at least one confirmed Th-cell epitope selected from the group consisting of SEQ ID NO: 686-845; 924-958, 1091-1140, and 1396-1466. A more preferred peptide according to the invention comprises at least 15 confirmed CTL epitopes and at least one confirmed Th-cell epitope; preferably at least 15 confirmed CTL epitopes selected from the group consisting of SEQ ID NO: 80-276, 278-314, 316-429, 432-483, 486-545, 548-636, 638-685; 846-923, 959-1090, and 1146-1395 and at least one confirmed Th-cell epitope selected from the group consisting of SEQ ID NO: 686-845; 924-95, 1091-1140, and 1396-1466. More preferably, a peptide according to the invention comprises at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65 or 70 confirmed CTL epitopes selected from the group consisting of SEQ ID NO: 80-276, 278-314, 316-429, 432-483, 486-545, 548-636, 638-685; 846-923, 959-1090, and 1146-1395 and at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20 confirmed Th-cell epitopes selected from the group consisting of SEQ ID NO: 686-845; 924-958, 1091-1140, and 1396-1466. Even more preferably, a peptide according to the invention comprises at least 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90 or 95 confirmed CTL epitopes selected from the group consisting of SEQ ID NO: 80-276, 278-314, 316-429, 432-483, 486-545, 548-636, 638-685; 846-923, 959-1090, and 1146-1395 and at least 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20 confirmed Th-cell epitopes selected from the group consisting of SEQ ID NO: 686-845; 924-958, 1091-1140, and 1396-1466. Preferably, a peptide according to the invention comprises at least 15 confirmed CTL epitopes as defined herein and at least 5 confirmed Th-cell epitopes as defined herein.

The HLA class I epitopes in the peptides according to the invention are preferably capable of being presented on HLA molecules being encoded by HLA alleles that are predominant in the population of human subjects to be treated. Preferred HLA class I epitopes in peptides according to the invention are epitopes capable of binding to: HLA-A0101; HLA-A0201; HLA-A0206; HLA-A0301; HLA-A1101; HLA-A2301; HLA-A2402; HLA-A2501; HLA-A2601; HLA-A2902; HLA-A3001; HLA-A3002; HLA-A3101; HLA-A3201; HLA-A3303; HLA-A6801; HLA-A6802; HLA-A7401; HLA-B0702; HLA-B0801; HLA-B1301; HLA-B1302; HLA-B1402; HLA-B1501; HLA-B1502; HLA-B1525; HLA-B1801; HLA-B2702; HLA-B2705; HLA-B3501; HLA-B3503; HLA-B3701; HLA-B3801; HLA-B3901; HLA-B4001; HLA-B4002; HLA-B4402; HLA-B4403; HLA-B4601; HLA-B4801; HLA-B4901; HLA-B5001; HLA-B5101; HLA-B5201; HLA-B5301; HLA-B5501; HLA-B5601; HLA-B5701; HLA-B5801 and HLA-B5802. In a preferred embodiment, a peptide of the invention, covers at least 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, or 100% of the HLA class I molecules that are encoded by HLA alleles predominant in the population of human subjects to be treated, wherein “Cover an HLA class I molecule” is understood herein as comprising a CTL epitope that shows binding affinity, preferably intermediate binding affinity, more preferably high binding affinity to said HLA class I molecule. Preferably, a peptide of the invention covers at least 10%, 20%, 30%, 40%, 50%, 60%, 70%, 80%, 90%, or 100% of group of HLA class I molecules consisting of: HLA-A0101; HLA-A0201; HLA-A0206; HLA-A0301; HLA-A1101; HLA-A2301; HLA-A2402; HLA-A2501; HLA-A2601; HLA-A2902; HLA-A3001; HLA-A3002; HLA-A3101; HLA-A3201; HLA-A3303; HLA-A6801; HLA-A6802; HLA-A7401; HLA-B0702; HLA-B0801; HLA-B1301; HLA-B1302; HLA-B1402; HLA-B1501; HLA-B1502; HLA-B1525; HLA-B1801; HLA-B2702; HLA-B2705; HLA-B3501; HLA-B3503; HLA-B3701; HLA-B3801; HLA-B3901; HLA-B4001; HLA-B4002; HLA-B4402; HLA-B4403; HLA-B4601; HLA-B4801; HLA-B4901; HLA-B5001; HLA-B5101; HLA-B5201; HLA-B5301; HLA-B5501; HLA-B5601; HLA-B5701; HLA-B5801 and HLA-B5802.

The HBV genome (SEQ ID NO: 3; see Table 1) consists of a partially double-stranded circular DNA molecule having four overlapping open reading frames (ORFs) that are responsible for the transcription and expression of seven different hepatitis B proteins through the use of multiple in-frame start codons. The HBV proteins are the core protein and the e antigen (HBeAg) encoded by the C gene, the HBV polymerase encoded by the P gene, the viral surface proteins (small (S), middle (M), and large (L)) encoded by the S gene, and X protein encoded by the X gene. There is an outer shell (or envelope) composed of several proteins known collectively as HBs or surface Proteins. This outer shell is frequently referred to as the surface coat. The outer surface coat surrounds an inner protein shell, composed of HBc protein. This inner shell is referred to as the core particle or capsid. Finally the core particle surrounds the viral DNA and the enzyme DNA polymerase.

The HBV core protein is the major component of the viral nucleocapsid. The amino acid sequences of the HBV polymerase, HBV core protein, HBV X protein and HBV large surface protein are represented by SEQ ID NO: 1, 4, 45 and 1141 respectively (see Table 1).

A preferred amino acid sequence of a human HBV polymerase protein is a sequence having at least 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 100% identity with the sequence depicted in SEQ ID NO: 1; a preferred coding sequence is a sequence having at least about 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 100% identity with the sequence depicted in SEQ ID NO: 2. A preferred amino acid sequence of an HBV core protein is a sequence having at least about 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 100% identity with the sequence depicted in SEQ ID NO: 4; a preferred coding sequence is a sequence having at least about 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 100% identity with the sequence depicted in SEQ ID NO: 5. A preferred amino acid sequence of an HBV large surface protein is a sequence having at least about 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 100% identity with the sequence depicted in SEQ ID NO: 1141, a preferred coding sequence is a sequence having at least 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 100% identity with the sequence depicted in SEQ ID NO: 1467.

The full length consensus amino acid sequence of the X protein was obtained by deducing the optimal sequence from the 39 published and reviewed full length (154 amino acid) HBV X protein amino acid sequences in the UniProt database (at: www.uniprot.org). These 39 sequences were first aligned and subsequently for each aa position the most frequently occurring aa was selected for that position in the consensus sequence. The 39 sequences with the following entries were included in the analysis: P69713; P03165; P0C686; P69714; Q8JMY5; Q69604; Q05499; O91531; Q9PX75; P20976; P20975; P20977; P24026; Q9PXA2; Q67923; P0C685; P0C678; O93195; Q9E6S8; P12936; Q91C38; Q913A9; Q8JMY3; Q8JN06; Q8JMZ5; Q69607; Q91B15; Q801U5; Q4R1S9; Q4R1S1; Q9YZR6; P0C687; Q9QMI3; P0C681; Q801U8; Q99HR6; P17102; Q67877; and Q69027 (see Table 2). A preferred consensus amino acid sequence of a human HBV X protein is a sequence having at least about 70%, 75%, 80%, 85%, 90%, 91%, 92%, 93%, 94%, 95%, 96%, 97%, 98%, 99%, 100% identity with the sequence depicted in SEQ ID NO: 45. The consensus amino acid sequence may be encoded by any coding sequence known or designed; the person skilled in the art knows how to design a coding sequence from a known amino acid sequence; such coding sequence may be a codon-optimized sequence. The terms “HBV X protein” and “consensus HBV X protein” are used interchangeably herein.

Percentage of identity is herein determined by calculating the ratio of the number of identical nucleotides/amino acids in the sequence divided by the length of the total nucleotides/amino acids of said sequence, minus the lengths of any gaps. Identity with a given SEQ ID NO means identity based on the full length of said sequence (i.e. over its whole length or as a whole).

Within the context of the present invention, “a peptide derived from an HBV protein” means that the peptide comprises at least 15 and at most 100 consecutive amino acids originating from the HBV core protein, HBV polymerase, HBV X consensus protein and/or HBV large surface protein. In other words, “a peptide derived from the HBV polymerase protein” comprises at most 100 consecutive amino acids of SEQ ID NO: 1, “a peptide derived from the HBV core protein” comprises at most 100 consecutive amino acids of SEQ ID NO: 4, “a peptide derived from the HBV X consensus protein” comprises at most 100 consecutive amino acids of SEQ ID NO: 45, and “a peptide derived from the HBV large surface protein” comprises at most 100 consecutive amino acids of SEQ ID NO: 1141. Preferably, “a peptide derived from the HBV polymerase protein” consists of at most 100 consecutive amino acids of SEQ ID NO: 1, “a peptide derived from the HBV core protein” consists of at most 100 consecutive amino acids of SEQ ID NO: 4, “a peptide derived from the HBV X consensus protein” consists of at most 100 consecutive amino acids of SEQ ID NO: 45, and “a peptide derived from the HBV large surface protein” consists of at most 100 consecutive amino acids of SEQ ID NO: 1141. Therefore, by definition, a peptide according to the invention is distinct from a full length HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein, as these full length proteins are all longer than 100 amino acids. Preferably, the peptide of the present invention is from about 15 to about 100 amino acids in length. More preferably the length of the peptide is from 15 up to 100 length indicated herein as the length of the peptide is 15-100 amino acids, or preferably the length of the peptide is 15-95 amino acids, or 15-90 amino acids, or 15-85 amino acids, or 15-70 amino acids, or 15-65 amino acids, or 15-60 amino acids, or 15-55 amino acids, or 15-50 amino acids, even more preferably 15-45 amino acids, even more preferably, 15-40 amino acids, even more preferably 17-39, even more preferably 19-43 amino acids, even more preferably 22-40 amino acids, even more preferably 28-40 and even more preferably 30-39 amino acids. Within the context of the present invention “a peptide which comprises at most 100 amino acids derived from an HBV protein” preferably means that the number of consecutive amino acids originating from an HBV protein, preferably being a protein selected from the group consisting of HBV core protein, HBV polymerase, HBV X consensus protein and HBV large surface protein and present in a peptide as defined herein, is 100, 99, 98, 97, 96, 95, 94, 93, 92, 91, 90, 89, 88, 87, 86, 85, 84, 83, 82, 81, 80, 79, 78, 77, 76, 75, 74, 73, 72, 71, 70, 69, 68, 67, 66, 65, 64, 63, 62, 61, 60, 59, 58, 57, 56, 55, 54, 53, 52, 51, 50, 49, 48, 47, 46, 45, 44, 43, 42, 41, 40, 39, 38, 37, 36, 35, 34, 33, 32, 31, or 30 amino acids or less. Within the context of the present invention “a peptide which comprises at least 15 amino acids derived from an HBV protein” preferably means that the number of consecutive amino acids originating from a protein selected from the group consisting of HBV core protein, HBV polymerase, HBV X consensus protein and HBV large surface protein and present in a peptide as defined herein, is at least 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44 or 45 amino acids. Within the context of the present invention “a peptide which comprises 15-100 amino acids derived from an HBV protein” preferably means that the number of consecutive amino acids originating from a protein selected from the group consisting of HBV core protein, HBV polymerase, HBV X consensus protein and HBV large surface protein and present in a peptide as defined herein, is at least 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44 or 45 amino acids and no more than 100, 99, 98, 97, 96, 95, 94, 93, 92, 91, 90, 89, 88, 87, 86, 85, 84, 83, 82, 81, 80, 79, 78, 77, 76, 75, 74, 73, 72, 71, 70, 69, 68, 67, 66, 65, 64, 63, 62, 61, 60, 59, 58, 57, 56, 55, 54, 53, 52, 51, 50, 49, 48, 47, 46, 45, 44, 43, 42, 41, 40, 39, 38, 37, 36, 35, 34, 33, 32, 31, or 30 amino acids. Within the context of the present invention “a peptide which comprises 15-100 amino acids derived from an HBV protein” preferably means that the number of consecutive amino acids originating from a protein selected from the group consisting of SEQ ID NO: 1, 4, 45 and 1141 and present in a peptide as defined herein, is at least 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44 or 45 amino acids and no more than about 100, 99, 98, 97, 96, 95, 94, 93, 92, 91, 90, 89, 88, 87, 86, 85, 84, 83, 82, 81, 80, 79, 78, 77, 76, 75, 74, 73, 72, 71, 70, 69, 68, 67, 66, 65, 64, 63, 62, 61, 60, 59, 58, 57, 56, 55, 54, 53, 52, 51, 50, 49, 48, 47, 46, 45, 44, 43, 42, 41, 40, 39, 38, 37, 36, 35, 34, 33, 32, 31, or 30 amino acids. More preferably, the length of the contiguous amino acid sequence from HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein comprised within the peptide is 15-100 amino acids, or preferably 15-95 amino acids, or 15-90 amino acids, or 15-85 amino acids, or 15-70 amino acids, or 15-65 amino acids, or 15-60 amino acids, or 15-55 amino acids, or 15-50 amino acids, even more preferably 15-45 amino acids, even more preferably, 15-40 amino acids, even more preferably 17-39, even more preferably 19-43 amino acids, even more preferably 22-40 amino acids, even more preferably 28-40 and even more preferably 30-39 amino acids. Even more preferably, the length of the contiguous amino acid sequence from the sequences selected from the group consisting of SEQ ID NO: 1, 4, 45 and 1141 comprised within the peptide is 15-100 amino acids, or preferably 15-95 amino acids, or 15-90 amino acids, or 15-85 amino acids, or 15-70 amino acids, or 15-65 amino acids, or 15-60 amino acids, or 15-55 amino acids, or 15-50 amino acids, even more preferably 15-45 amino acids, even more preferably, 15-40 amino acids, even more preferably 17-39, even more preferably 19-43 amino acids, even more preferably 22-40 amino acids, even more preferably 28-40 and even more preferably 30-39 amino acids. A peptide according to the invention may comprise additional amino acids than the ones originating from an HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein or may entirely be made of or consist of an amino acid sequence originating from a protein selected from the group consisting of HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein. A peptide according to the invention may comprise several parts of non-contiguous amino acid sequences from an HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein, wherein it is to be understood that said peptide has a length, a TRIA score and/or amount and type of T cell epitopes as defined herein.

According to one embodiment, a peptide according to the invention consists of any of the contiguous amino acid sequence from HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein as defined herein and indicated by its representing SEQ ID NO, whereby it is understood that no amino acids are appended to either end of the said peptide.

According to another embodiment, the peptide according to the invention comprises any of the contiguous amino acid sequences from HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein as defined herein and indicated by its representing SEQ ID NO and further may comprise a modified amino acid and/or a covalently linked functional group such as a fluorinated group, a human toll-like receptor ligand and/or agonist, an oligonucleotide conjugate, PSA, a sugar chains or glycan, a pam3cys and/or derivative thereof, preferably a pam3cys lipopeptide or variant or derivative thereof, preferably such as described in WO2013051936A1, CpG oligodeoxynucleotides (CpG-ODNs), Cyclic dinucleotides (CDNs), 2-aminoisobutyric acid (Abu), Muramyl dipeptide (MDP), a DC pulse cassette, a tetanus toxin derived peptide.

In an embodiment, the peptide of the invention comprises or consists of a non-naturally occurring sequence as a result of the synthesis of non-natural lengths or as a result of comprising additional amino acids not originating from an HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein or as a result of comprising non-contiguous amino acid sequences from an HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein, and/or as a result of comprising a modified amino acid and/or a non-naturally occurring amino acid and/or a covalently linked functional group such as a fluorinated group, a fluorcarbon group, a human toll-like receptor ligand and/or agonist, an oligonucleotide conjugate, PSA, a sugar chains or glycan, a pam3cys and/or derivative thereof preferably such as described in WO2013051936A1, CpG oligodeoxynucleotides (CpG-ODNs), Cyclic dinucleotides (CDNs), a DC pulse cassette, a tetanus toxin derived peptide, a human HMGB1 derived peptide; either within the peptide or appended to the peptide, as indicated above. The peptide of the invention may comprise 2-aminoisobutyric acid (Abu, an isostereomer of cysteine). A cysteine of the peptide of the invention may be replaced by Abu. Encompassed within the present invention is a peptide of SEQ ID NO: 77, wherein the N-terminal cysteine has been replaced by Abu.

Preferably, a peptide of the invention is an isolated peptide, wherein “isolated” does not reflect the extent to which the peptide is purified, but indicates that the peptide has been removed from its natural milieu (i.e., that has been subject to human manupilation), and may be a recombinantly produced peptide or a synthetically produced peptide.

Preferably, the invention relates to a peptide that can be effectively used in the prevention, partial clearance and/or treatment or full clearance of a HBV related disease or condition in a subject, preferably as detectable by:

-   -   an activation or an induction of the immune system and/or an         increase in HBV specific activated CD4⁺ and/or CD8⁺ T-cells in         peripheral blood or an increase of the cytokines produced by         these T-cells after at least one week of treatment; and/or     -   an inhibition of proliferation of HBV infection or a detectable         decrease of HBV infected cells or a decrease in cell viability         of HBV infected cells; and/or     -   an induction or increased induction of HBV infected cell death;         and/or     -   an inhibition or prevention of the increase of HBV infected         cells.

In all embodiments of the present invention, a subject is preferably a mammal, more preferably a human. A subject may be an animal model, preferably a non-human mammalian model with humanized HLA class I and class II molecules, or a mammalian, preferably human, organ, such as a liver.

In all embodiments of the present invention, the term “HBV related disease or condition” is preferably defined as acute HBV infection, chronic HBV infection and other conditions where the hepatitis virus is found in the blood or body fluids containing blood of a subject, such as liver cirrhosis and liver cancer, or optionally of an asymptomatic subject that is characterized by the presence of the virus in the body of said subject.

In the context of the invention, a patient may survive and may be considered as being disease free as a consequence of treatment according to the invention. Alternatively, the disease or condition may have been stopped or regressed (i.e. cleared or partially cleared infection). A significant increase of HBV-specific activated CD4⁺ or CD8⁺ cells in peripheral blood at least one week after vaccination is preferably at least a 5%, 10%, 20%, 30% increase or more. An inhibition of the proliferation of HBV infected cells is preferably at least 5%, 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75% inhibition or more. An induction of HBV infected cell death may be at least 1%, 2%, 3%, 4%, 5%, 6%, 7%, 8%, 9%, 10%, 15%, 20%, 25%, or more. HBV infection may be inhibited at least 5%, 10%, 20%, 30%, 40%, 50%, 55%, 60%, 65%, 70% or 75% induction, or more. HBV infected cells may be reduced by at least 5%, 10%, 15%, 20%, 25%, 30%, 35%, 40%, 45%, 50%, 55%, 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95%, 98% or 100%.

In each embodiment, within this or further aspects disclosed herein, wherein the effect of a peptide according to the invention, a composition according to the invention, a polynucleotide according to the invention, a viral vector comprising a polynucleotide according to the invention and/or a cell according to the invention and/or a cell obtained or obtainable by a method according to the invention, is quantified, the assay may be carried out by comparison to a subject not treated or to the same subject before treatment.

Acute and chronic HBV infection can be treated using the present invention. A peptide according to the invention comprising epitopes which are to be presented to T-cell receptors of CD8⁺ cytotoxic T cells and/or CD4⁺ T-helper cells preferably fulfill a number of structural requirements as defined herein. In vitro and ex vivo T cell experiments are preferably used to confirm the capability of peptides according to the invention to induce substantial CD4⁺ T-helper and CD8⁺ cytotoxic T cell responses. The peptides of the present invention thereby provide a marked improvement in the selection of relatively short peptides that may be chemically synthesized, comprising the most potent and most widely applicable HLA class I and/or class II presented T cell epitopes derived from HBV.

In an embodiment, a peptide is distinct from a contiguous sequence of amino acids of HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein.

A peptide according to the invention comprising a T-cell epitope from HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein, may be modified by deletion or substitution of one or more amino acids, by extension at the N- and/or C-terminus with additional amino acids or functional groups, which may improve bio-availability, targeting to T-cells, or comprise or release immune modulating substances that provide adjuvant or (co) stimulatory functions. The optional additional amino acids at the N- and/or C-terminus are preferably not present in the corresponding positions in the native amino acid sequence of HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein.

A peptide according to the invention comprising a T-cell epitope is obtainable by chemical synthesis and subsequent purification according to methods well-known in the art. (see e.g. Atherton et al., 1989; Barany et al., 1979; Fields et al., 1997). A peptide according to the invention is preferably soluble in physiologically acceptable watery solutions (e.g. PBS) comprising no more than 35, 20, 10, 5 or 0% DMSO. In such a solution the peptide according to the invention is preferably soluble at a concentration of at least 0.5, 1, 2, 4, or 8 mg peptide per ml. More preferably, a mixture of more than one different peptide according to the invention is soluble at a concentration of at least 0.5, 1, 2, 4, or 8 mg peptide per ml in such solutions.

The peptides according to the invention may be easily synthesized and are large enough to be taken up by professional antigen presenting cells, in particular dendritic cells (DC), processed by the proteasome and/or the endosomal/lysosomal degradation and antigen processing system and preferably have sufficient length to contain at least 1, 5, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 73, 75, 80, 85, 90, 95, 100, 105, 110, 115, 120, 125, 130, 135, 140, 145, 150, 155, 160, 165, 170 to preferably up to 175 CTL epitopes and/or at least 1, 5, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85, 90, 95 to preferably up to 96 Th-cell epitopes as defined herein. Optionally, a peptide according to the invention may comprise N- or C-terminal extensions, which may be amino acids, modified amino acids or other functional groups that may for instance enhance bio-availability, cellular uptake, processing and/or solubility.

Preferably, a peptide according to the invention is a peptide comprising a peptide with an amino acid sequence selected from the group consisting of:

-   -   a fragment of 15 to 30 amino acids of SEQ ID NO: 51, preferably         contiguous amino acids,     -   a fragment of 15 to 35 amino acids of SEQ ID NO: 52, preferably         contiguous amino acids,     -   a fragment of 15 to 33 amino acids of SEQ ID NO: 53, preferably         contiguous amino acids,     -   a fragment of 15 to 33 amino acids of SEQ ID NO: 54, preferably         contiguous amino acids,     -   a fragment of 15 to 39 amino acids of SEQ ID NO: 55, preferably         contiguous amino acids,     -   a fragment of 15 to 35 amino acids of SEQ ID NO: 56, preferably         contiguous amino acids,     -   a fragment of 15 to 34 amino acids of SEQ ID NO: 57, preferably         contiguous amino acids,     -   a fragment of 15 to 32 amino acids of SEQ ID NO: 58, preferably         contiguous amino acids,     -   a fragment of 15 to 33 amino acids of SEQ ID NO: 59, preferably         contiguous amino acids,     -   a fragment of 15 to 38 amino acids of SEQ ID NO: 60, preferably         contiguous amino acids,     -   a fragment of 15 to 38 amino acids of SEQ ID NO: 61, preferably         contiguous amino acids,     -   a fragment of 15 to 33 amino acids of SEQ ID NO: 62, preferably         contiguous amino acids,     -   a fragment of 15 to 34 amino acids of SEQ ID NO: 63, preferably         contiguous amino acids,     -   a fragment of 15 to 36 amino acids of SEQ ID NO: 64, preferably         contiguous amino acids,     -   a fragment of 15 to 34 amino acids of SEQ ID NO: 65, preferably         contiguous amino acids,     -   a fragment of 15 to 34 amino acids of SEQ ID NO: 66, preferably         contiguous amino acids,     -   a fragment of 15 to 34 amino acids of SEQ ID NO: 67, preferably         contiguous amino acids,     -   a fragment of 15 to 39 amino acids of SEQ ID NO: 68, preferably         contiguous amino acids,     -   a fragment of 15 to 35 amino acids of SEQ ID NO: 69, preferably         contiguous amino acids,     -   a fragment of 15 to 32 amino acids of SEQ ID NO: 70, preferably         contiguous amino acids,     -   a fragment of 15 to 38 amino acids of SEQ ID NO: 71, preferably         contiguous amino acids,     -   a fragment of 15 to 36 amino acids of SEQ ID NO: 72, preferably         contiguous amino acids,     -   a fragment of 15 to 36 amino acids of SEQ ID NO: 73, preferably         contiguous amino acids,     -   a fragment of 15 to 35 amino acids of SEQ ID NO: 74, preferably         contiguous amino acids,     -   a fragment of 15 to 34 amino acids of SEQ ID NO: 75, preferably         contiguous amino acids,     -   a fragment of 15 to 33 amino acids of SEQ ID NO: 76, preferably         contiguous amino acids,     -   a fragment of 15 to 35 amino acids of SEQ ID NO: 77, preferably         contiguous amino acids,     -   a fragment of 15 to 35 amino acids of SEQ ID NO: 78, preferably         contiguous amino acids,     -   a fragment of 15 to 34 amino acids of SEQ ID NO: 79, preferably         contiguous amino acids,     -   a fragment of 15 to 34 amino acids of SEQ ID NO: 1142,         preferably contiguous amino acids,     -   a fragment of 15 to 34 amino acids of SEQ ID NO: 1143,         preferably contiguous amino acids,     -   a fragment of 15 to 34 amino acids of SEQ ID NO: 1144,         preferably contiguous amino acids,     -   a fragment of 15 to 36 amino acids of SEQ ID NO: 1145,         preferably contiguous amino acids,     -   a fragment of 15 to 32 amino acids of SEQ ID NO: 1468,         preferably contiguous amino acids,     -   a fragment of 15 to 31 amino acids of SEQ ID NO: 1469,         preferably contiguous amino acids,     -   a fragment of 15 to 30 amino acids of SEQ ID NO: 1470,         preferably contiguous amino acids,     -   a fragment of 15 to 31 amino acids of SEQ ID NO: 1471,         preferably contiguous amino acids, and;

wherein the length of the preferably contiguous amino acid sequence is preferably at least 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32 or 33 amino acids and/or preferably no more than 45, 44, 43, 42, 41, 40, 39, 38, 37, 36, 35, 34, 33, 32, 31, 30, 29, 28, 27, 26, 25, 24, 23, 22, 21, 20, 19, 18, 17, 16, 15 amino acids, most preferably a length of 30-39 amino acids.

In a second aspect, the invention provides a polynucleotide encoding a peptide according to the invention, preferably a peptide as defined herein above. A polynucleotide may be any polynucleotide comprising e.g. RNA, DNA, and/or cDNA; a polynucleotide may be single stranded or double stranded and may comprise nucleotide analogues and/or nucleotide equivalents such as a peptide nucleic acid (PNA) and a morpholino nucleotide analogue. A polynucleotide may be codon optimized for a host of choice to facilitate expression of the encoded subject matter.

The polynucleotide according to the invention does not encode a wild-type full length HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein, but rather encode a peptide according to the invention as such, or flanked by amino acid sequence that are not contiguous with a wild-type HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein. Such flanking amino acids may be from proteins other than a wild-type HBV and/or they may be from other locations within a wild-type HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein that are not contiguous with the peptide they flank. Preferably, the polynucleotide encodes two or more peptides according to the invention arranged as beads-on-string, whereby the peptides according to the invention (the beads) are linked directly together and/or are linked through linker sequences that are from proteins other than a wild-type HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein, and/or from other locations within a wild-type HBV core protein, HBV polymerase, HBV X protein and/or HBV large surface protein, that are not contiguous with the peptide they flank. The amino acid sequences flanking or linking the peptides may comprise proteolytic cleavage sites. A polynucleotide according to the invention may be applied to deliver a peptide according to the invention in various ways. A polynucleotide according to the invention may e.g. be used in the production of recombinant protein or peptide in a suitable host cell (e.g. a bacterial host cell such as E. coli, a suitable yeast host cell such as S. cerevisiae, a suitable filamentous fungal such as an Aspergillus or mammalian host cell) from which the recombinant protein or peptide may be purified. Alternatively the polynucleotide may be operably linked to expression regulatory sequences (promoters and the like) and incorporated in an expression construct for human cells. Such (autologous) cells may be transfected or transduced ex vivo to be (re)-administered to a subject in need thereof. Alternatively such expression construct according to the invention may be incorporated into a suitable gene therapy vector. Viral vectors (based on a defective virus) are more efficient agents for gene transfer as compared to non-viral agents. Suitable viral expression constructs include e.g. vectors that are based on adenovirus, adeno-associated virus (AAV), retroviruses or modified vaccinia Ankara (MVA). The polynucleotide according to the invention may also be operably linked to a sequence encoding and adjuvant such as a Toll-like receptor (TLR) ligand, a NOD ligand, or a RIG-I ligand.

In a third aspect, the present invention provides a cell comprising the polynucleotide according to the second aspect of the invention. Such cell can be used for e.g. production of a peptide according to the invention or for medical purposes such as prevention and/or treatment of an HBV related disease as defined elsewhere herein. Said cell may be any host cell. For the specific applications such as described here above, the selection of the host cell may be made according to such use. The host cell may be a prokaryote or may be a eukaryote. A preferred prokaryote cell is E. coli. When the cell is a eukaryote, the cell preferably is a mammalian, insect, plant, fungal, or algal cell. Preferred mammalian cells include e.g. Chinese hamster ovary (CHO) cells, COS cells, 293 cells, PerC6 cells, and antigen presenting cells such as dendritic cells. Preferred insect cells include e.g. Sf9 and Sf21 cells and derivatives thereof. Preferred fungal cells include Candida, Hansenula, Kluyveromyces, Pichia, Saccharomyces, Schizosaccharomyces, Yarrowia and filamentous fungal cells. Most preferably, the eukaryotic cell is a human antigen presenting cell, preferably a dendritic cell.

Methods to introduce a polynucleotide into a cell are known to the person skilled in the art. When expression of the polynucleotide is desired, the person skilled in the art knows how to achieve such; the polynucleotide may e.g. be provided with proper control sequences such as a promoter and terminator sequence and may be inserted into a proper vector such as a plasmid or a method described in the second aspect of the invention may be used.

The present invention also provides for an antigen presenting cell such as a dendritic cell as defined earlier herein that has been contacted and/or loaded with a peptide according to the invention, preferably a peptide according to the first aspect of the present invention. Such preferably autologous dendritic cell may be used for immune therapeutic treatment of a subject in need thereof. Such dendritic cell can be isolated from the subject, loaded with at least one peptide according to the invention and used for treatment.

In a fourth aspect, the present invention provides a method for the preparation of an HBV specific T-cell, said method comprising contacting a T-cell with an antigen presenting cell expressing a polynucleotide according to the invention and/or contacting a T-cell with an antigen presenting cell loaded with a peptide according to the invention; and, optionally, culturing said T-cell. The T-cell is preferably a CD8⁺ cytotoxic T-cell or a CD4⁺ T-helper cell.

Contacting a cell with a polynucleotide may be performed using any method known to the person skilled in the art, preferably a polynucleotide according to the invention is introduced into the antigen presenting cell (APC), preferably a dendritic cell, using transfection. Before contacting, the polynucleotide according to the invention may be provided with proper control sequences, or be comprised into a proper vector such as described elsewhere herein.

Contacting a T-cell with a peptide according to the invention can be performed by any method known to the person skilled in the art. Preferably, a peptide or an epitope comprised in a peptide is presented to the CD8⁺ cytotoxic T-cell or CD4⁺ T-helper cell by an HLA class I or an HLA class II molecule on the surface of an antigen presenting cell, preferably a dendritic cell. The person skilled in the art knows how to load an antigen presenting cell with a peptide.

Culturing said T-cell may be performed using any method known by the person skilled in the art. Maintaining a T-cell under conditions to keep the cell alive is herein also to be construed to be culturing.

Preferably, the T-cell according to this aspect of the invention is contacted with a peptide according to the invention as defined in the first aspect of the invention.

In a fifth aspect, the present invention provides a T-cell obtainable by the method depicted in the fourth aspect of the present invention. Preferably, such T-cell is a T-cell that is obtained by the method according to the fourth aspect of the invention. The T-cell is preferably a CD8⁺ cytotoxic T-cell or a CD4⁺ T-helper cell.

Preferably, the T-cell according to this aspect of the invention has been contacted with a peptide according to the invention as defined in the first aspect of the invention.

In a sixth aspect, the present invention provides a composition useful for the prevention and/or treatment of an HBV related disease or related condition, comprising a peptide according to the invention and/or a polynucleotide according to the invention and/or a cell, preferably a T-cell, according to the invention and/or a cell, preferably a T-cell, obtained by the method according to the fourth aspect of the invention and a pharmaceutically acceptable carrier.

When comprising a peptide according to the invention, the composition according to the invention preferably comprises at least 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32 and up to 33 different peptides according to the invention. Preferably, a composition according to the invention comprises a peptide according to the invention as defined in the first aspect of the invention. In a preferred embodiment, a composition of the invention comprises a combination of peptides wherein said combination of peptides covers at least 70%, 80%, 90%, 92%, 94%, 95%, 96%, 97%, 98%, 99% or 100% of the HLA class I molecules that are encoded by HLA alleles predominant in the population of human subjects to be treated as defined herein above.

When comprising a polynucleotide according to the present invention, the composition according to the invention preferably comprises at least 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32 and up to 33 different polynucleotides according to the invention. Preferably, a composition according to the invention comprises a polynucleotide according to the invention as defined in the second aspect of the invention.

When comprising a cell according to the invention, the composition according to the invention preferably comprises at least 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32 and up to 33 different cells, preferably T-cells that have been contacted with a peptide according to the invention. Preferably, said T-cells have been contacted with a peptide according to the invention as defined in the first aspect of the invention. The T-cell is preferably a CD8⁺ cytotoxic T-cell or a CD4⁺ T-helper cell.

In a preferred embodiment, the composition of the invention comprises at least 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32 and up to 33 different peptides of the peptides consisting of or comprising of a peptide selected from the group consisting of SEQ ID NO: 51-79, 1142-1145 and 1468-1471, more preferably selected from the group consisting of SEQ ID NO: 51, 55, 60, 63, 64, 68, 71, 74, 75, 76, 77, 1142 and 1469, more preferably selected from the group consisting of SEQ ID NO: 51, 55, 60, 63, 64, 68, 71, 74, 75, 77, 1142 and 1469, even more preferably selected from the group consisting of SEQ ID NO: 55, 60, 63, 64, 68, 71, 74, 75, 76, 77 and 1469, even more preferably selected from the group consisting of SEQ ID NO: 55, 60, 63, 64, 68, 71, 74, 75, 77 and 1469, even more preferably selected from the group consisting of SEQ ID NO: 60, 63, 71, 74, 75 and 1469, most preferably selected from the group of SEQ ID NO: 75, 1469 and 63. Further preferred is a composition that comprises at least 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32 and up to 33 different peptides of the peptides consisting of or comprising of a peptide selected from the group consisting of SEQ ID NO: 51, 60, 63, 64, 68, 71, 74-77, more preferably selected from the group consisting of SEQ ID NO: 63, 71 and 75.

In a preferred embodiment, the composition of the invention comprises at least a peptide that comprises or consists of a peptide of SEQ ID NO: 63 and peptide that comprises or consists of a peptide of SEQ ID NO: 1143.

Also preferred is a composition that comprises at least a peptide that comprises or consists of a peptide of SEQ ID NO: 63 and peptide that comprises or consists of a peptide of SEQ ID NO: 75.

Also preferred is a composition that comprises at least a peptide that comprises or consists of a peptide of SEQ ID NO: 1143 and peptide that comprises or consists of a peptide of SEQ ID NO: 75.

Also preferred is a composition that comprises at least a peptide that comprises or consists of a peptide of SEQ ID NO: 71 and peptide that comprises or consists of a peptide of SEQ ID NO: 75.

Also preferred is a composition that comprises at least a peptide that comprises or consists of a peptide of SEQ ID NO: 71 and peptide that comprises or consists of a peptide of SEQ ID NO: 63.

Also preferred is a composition that comprises at least a peptide that comprises or consists of a peptide of SEQ ID NO: 1144 and peptide that comprises or consists of a peptide of SEQ ID NO: 63.

Also preferred is a composition that comprises at least a peptide that comprises or consists of a peptide of SEQ ID NO: 1144 and peptide that comprises or consists of a peptide of SEQ ID NO: 75.

Also preferred is a composition that comprises at least a peptide that comprises or consists of a peptide of SEQ ID NO: 1144 and peptide that comprises or consists of a peptide of SEQ ID NO: 1143.

Also preferred is a composition that comprises at least a peptide that comprises or consists of a peptide of SEQ ID NO: 63, a peptide that comprises or consists of a peptide of SEQ ID NO: 1143, and a peptide that comprises or consists of a peptide of SEQ ID NO: 75.

Also preferred is a composition that comprises at least a peptide that comprises or consists of a peptide of SEQ ID NO: 63, a peptide that comprises or consists of a peptide of SEQ ID NO: 1143, a peptide that comprises or consists of a peptide of SEQ ID NO: 75, and a peptide that comprises or consists of a peptide of SEQ ID NO: 1144. Also preferred is a composition that comprises at least a peptide that comprises or consists of a peptide of SEQ ID NO: 75, and a peptide that comprises or consists of a peptide of SEQ ID NO: 1469. Also preferred is a composition that comprises at least a peptide that comprises or consists of a peptide of SEQ ID NO: 63, and a peptide that comprises or consists of a peptide of SEQ ID NO: 1469.

Also preferred is a composition that comprises at least a peptide that comprises or consists of a peptide of SEQ ID NO: 75, a peptide that comprises or consists of a peptide of SEQ ID NO: 1469, and a peptide that comprises or consists of a peptide of SEQ ID NO: 63. Preferably, said composition further comprising a peptide that comprises or consists of a peptide of SEQ ID NO: 60 and/or that comprises or consists of a peptide of SEQ ID NO: 71, and/or that comprises or consists of a peptide of SEQ ID NO: 74.

A preferred composition of the invention comprises a peptide that consists of or comprises a peptide of SEQ ID NO: 75, a peptide that consists of or comprises a peptide of SEQ ID NO: 63, and a peptide that consists of or comprises a peptide of SEQ ID NO: 1469

A preferred composition of the invention comprises a peptide that consists of or comprises a peptide of SEQ ID NO: 75, a peptide that consists of or comprises a peptide of SEQ ID NO: 63, and a peptide that consists of or comprises a peptide of SEQ ID NO: 71.

A pharmaceutically acceptable carrier can be any such carrier known to the person skilled in the art, e.g. buffered aqueous solutions at physiological ionic strength and/or osmolarity (such as e.g. PBS).

Preferably, a composition according to the present invention further comprises at least one adjuvant. Such adjuvant may be any adjuvant known to the person skilled in the art. Preferred adjuvants are defined later herein.

A preferred use of a peptide, polynucleotide, composition, cell and/or T-cell according to the invention or a T-cell obtainable or obtained by a method according to the invention is the use as a medicament. A specific preferred use of a peptide, polynucleotide, composition, cell and/or T-cell according to the invention or a T-cell obtainable or obtained by a method according to the invention is for the treatment and/or prevention of an HBV related disease or condition. Accordingly, the invention provides for the use of a peptide, polynucleotide, composition, cell and/or T-cell according to the invention or a T-cell obtainable or obtained by a method according to the invention for the manufacturing of a medicament for the treatment and/or prevention of an HBV related disease.

The invention further provides a method for the prevention and/or treatment of an HBV related disease or condition comprising administering to a subject an effective amount of a peptide, polynucleotide, composition, cell or T-cell according to the invention and/or a T-cell obtainable or obtained by a method according to the invention.

Formulation of medicaments, ways of administration and the use of pharmaceutically acceptable excipients are known and customary in the art and for instance described in Remington; The Science and Practice of Pharmacy, 21^(st) Edition 2005, University of Sciences in Philadelphia. Pharmaceutical compositions and medicaments according to the invention are preferably formulated to be suitable for intravenous or subcutaneous, or intramuscular administration, although other administration routes can be envisaged, such as mucosal administration or intradermal and/or intracutaneous administration, e.g. by injection. Intradermal administration is preferred herein. Advantages and/or preferred embodiments that are specifically associated with intradermal administration are later on defined in a separate section entitled “intradermal administration”.

It is furthermore encompassed by the present invention that the administration of a peptide, a polynucleotide, a composition and/or a cell according to the invention and/or a cell obtainable or obtained by a method according to the invention with an appropriate pharmaceutical excipient such as an adjuvant and/or a carrier may be carried out as a single administration. Alternatively, the administration may be repeated if needed and/or distinct peptides, polynucleotides, compositions and/or cells according to the invention and/or cells obtainable or obtained by a method according to the invention with appropriate pharmaceutical excipients such as adjuvants and/or carriers, may be sequentially administered.

The peptide, polynucleotide, composition and/or cell according to the invention and/or cell obtainable or obtained by a method according to the invention (also referred to as medicaments according to the invention) may preferably comprise at least one immune response stimulating compound or adjuvant. Advantageously the medicaments according to the invention may additionally comprise one or more synthetic adjuvants. Such adjuvant may be admixed to the medicament according to the invention or may be administered separately to the subject, mammal or human, to be treated. Particularly preferred are those adjuvants that are known to act via the Toll-like receptors and/or via a RIG-I (Retinoic acid—Inducible Gene-1) protein and/or via an endothelin receptor. Immune modifying compounds that are capable of activation of the innate immune system can be activated particularly well via Toll like receptors (TLRs), including TLRs 1-10. Compounds capable of activating TLR receptors and modifications and derivatives thereof are well documented in the art. TLR1 may be activated by bacterial lipoproteins and acetylated forms thereof, TLR2 may in addition be activated by Gram positive bacterial glycolipids, LPS, LPA, LTA, fimbriae, outer membrane proteins, heat shock proteins from bacteria or from the host, and Mycobacterial lipoarabinomannans. TLR3 may be activated by dsRNA, in particular of viral origin, or by the chemical compound poly(I:C). TLR4 may be activated by Gram negative LPS, LTA, Heat shock proteins from the host or from bacterial origin, viral coat or envelope proteins, taxol or derivatives thereof, hyaluronan containing oligosaccharides and fibronectins. TLR5 may be activated with bacterial flagellae or flagellin. TLR6 may be activated by mycobacterial lipoproteins and group B Streptococcus heat labile soluble factor (GBS-F) or Staphylococcus modulins. TLR7 may be activated by imidazoquinolines, such as imiquimod, resiquimod and derivatives imiquimod or resiquimod. TLR9 may be activated by unmethylated CpG DNA or chromatin—IgG complexes. In particular TLR3, TLR7 and TLR9 play an important role in mediating an innate immune response against viral infections, and compounds capable of activating these receptors are particularly preferred for use in the methods of treatment and in the compositions or medicaments according to the invention. Particularly preferred adjuvants comprise, but are not limited to, synthetically produced compounds comprising dsRNA, poly(I:C), unmethylated CpG DNA which trigger TLR3 and TLR9 receptors, IC31, a TLR 9 agonist, IMSAVAC, a TLR 4 agonist, Montanide ISA-51, Montanide ISA 720 (an adjuvant produced by Seppic 7, France). RIG-I protein is known to be activated by dsRNA just like TLR3 (Kato et al, 2005). A particularly preferred TLR ligand is a pam3cys and/or derivative thereof, preferably a pam3cys lipopeptide or variant or derivative thereof, preferably such as described in WO2013051936A1. Further preferred adjuvants are Cyclic dinucleotides (CDNs), Muramyl dipeptide (MDP) and poly-ICLC. In a preferred embodiment, the adjuvants of the invention are non-naturally occurring adjuvants such as the pam3cys lipopeptide derivative as described in WO2013051936A1, Poly-ICLC, imidazoquinoline such as imiquimod, resiquimod or derivatives thereof, CpG oligodeoxynucleotides (CpG-ODNs) having a non-naturally occurring sequence, and peptide-based adjuvants, such as muramyl dipeptide (MDP) or tetanus toxoid peptide, comprising non-naturally occurring amino acids.

In another preferred embodiment, the synthetic adjuvant compounds are physically linked to the peptides of the invention. Physical linkage of adjuvants and costimulatory compounds or functional groups to the HLA class I and HLA class II epitope comprising peptides provides an enhanced immune response by improved targeting to antigen-presenting cells, in particular dendritic cells, that internalize, metabolize and display antigen and by simultaneously stimulating such cells to upregulate expression of a variety of co-stimulatory molecules, thereby becoming efficient T cell response inducing and enhancing cells. Another preferred immune modifying compound is an inhibitor of an endothelin receptor such as BQ-788 (Buckanovich R J et al., 2008; Ishikawa K, 1994). BQ-788 is N-cis-2,6-dimethylpiperidinocarbonyl-L-gamma-methylleucyl-D-1-methoxycarbonyltryptophanyl-D-norleucine. However any derivative of BQ-788 or modified BQ-788 compound is also encompassed within the scope of this invention. Another preferred immune response stimulating compound or adjuvant is Interferon alpha (IFNα), more preferably pegylated Interferon alpha, which may be admixed to the medicament according to the invention, or may be administered separately to the subject as an immuno-modulatory agent. It is to be construed herein that when an immune response stimulating compound is admixed to the medicament according to the invention, it is depicted as an adjuvant; when administered separately, it is depicted as an immuno-modulatory agent, or an immuno-modulator, which terms are used herein interchangeably. Furthermore, the use of antigen presenting cell (co)stimulatory molecules, as set out in WO99/61065 and in WO03/084999, in combination with the peptides and compositions of the invention is preferred. In particular the use of 4-1BB and/or CD40 ligands, agonistic antibodies, OX40 ligands, CD27 ligands or functional fragments and derivatives thereof, as well as synthetic compounds with similar agonistic activity are preferably administered separately or combined with the peptides of the invention to subjects to be treated in order to further stimulate the mounting of an optimal immune response in the subject.

In addition, a preferred embodiment comprises delivery of the medicaments according to the invention, with or without additional immune stimulants such as TLR ligands and/or anti CD40/anti-4-1BB/anti-OX-40 or anti-CD27 antibodies in a slow release vehicle such as mineral oil (e.g. Montanide ISA 51) or PLGA. Alternatively, the medicament according to the invention may be delivered intradermally, e.g. by injection, with or without immune stimulants (adjuvants and/or immuno-modulators). Preferably, for intradermal delivery the medicaments according to the invention are administered in a composition consisting of the medicaments and one or more immunologically inert pharmaceutically acceptable carriers, e.g. buffered aqueous solutions at physiological ionic strength and/or osmolarity (such as e.g. PBS).

In a preferred embodiment, a medicament according to the invention as defined herein is formulated to be suitable for intradermal administration or application. Intradermal is known to the skilled person. In the context of the invention, intradermal is synonymous with intradermal and is distinct from subcutaneous. A most superficial application of a substance is epicutaneous (on the skin), then would come an intradermal application (in or into the skin), then a subcutaneous application (in the tissues just under the skin), then an intramuscular application (into the body of the muscle). An intradermal application is usually given by injection. An intradermal injection of a substance can be done to test a possible reaction, allergy and/or cellular immunity to it, but can also be performed to elicit a specific antibody or T cell immune response. A subcutaneous application is usually also given by injection: a needle is injected in the tissues under the skin.

The advantage of intradermal administration is that the formulation procedure can be simplified and be made more robust. Furthermore, intradermal vaccine delivery has been repeatedly shown to allow significant dose sparing for eliciting vaccine-induced antibody or T cell responses when compared to conventional administration methods such as intramuscular and subcutaneous administration. This effect is attributed to the relatively dense network of immune cells present in the skin. This was also shown with the HPV16 synthetic long peptides in a human study published by Van der Burg et al. (2007). In this study it was shown that intradermal injection of pools of HPV16 synthetic long peptides is safe and results in the migration of HPV16-specific T cells into the skin as well as in an increase in the number of HPV16-specific T cells circulating in the blood.

In an embodiment, a medicament according to the invention does not comprise any adjuvant such as Montanide ISA-51, and specifically Montanide ISA-51. This means that the formulation of the medicament is more simple: an oil-water based emulsion is preferably also not present in a medicament according to the invention. Accordingly, a medicament according to the invention preferably does not comprise an adjuvant such as Montanide ISA-51 and specifically Montanide ISA-51 and/or does not comprise an oil-in-water based emulsion; more preferably a medicament according to the invention comprises neither of these to adjuvant and even more preferably comprises no adjuvant at all. Therefore, in an embodiment, the medicament according to the invention is a, preferably buffered, aqueous solution, preferably at physiological ionic strength and/or osmolality, such as e.g. PBS (Phosphate Buffer Saline) or water for injection (WFI), comprising or consisting of one or more medicaments as defined earlier herein. The skilled person knows how to prepare such a solution.

A medicament according to the invention has another advantage, which is that by intradermally administering low amounts of a medicament, preferably a peptide as earlier herein defined, an immunogenic effect may still be achieved. The amount of each peptide used is preferably ranged from 1 and 1000 μg, more preferably from 5 and 500 μg, even more preferably from 10 and 100 μg.

In an embodiment, the medicament according to the invention comprises a peptide as earlier defined herein and at least one adjuvant, said adjuvant being not formulated in an oil-in water based emulsion and/or not being of an oil-in-water emulsion type as earlier defined herein. This type of medicament according to the invention may be administered as a single administration. Alternatively, the administration of a peptide as earlier herein defined and/or an adjuvant may be repeated if needed and/or distinct peptides and/or distinct adjuvants may be sequentially administered. It is further encompassed by the present invention that a peptide according to the invention is administered intradermally whereas an adjuvant as defined herein is sequentially administered. The adjuvant may be intradermally administered. However any other way of administration may be used for the adjuvant. Intradermal administration of a peptide may be attractive since typically and depending on the disease, the injection of the vaccine is realized at or as close by as possible to the site of the disease resulting in the local activation of the disease draining lymph node, resulting in a stronger local activation of the immune system. A preferred immune response stimulating compound (immuno-modulator) or adjuvant for intradermal administration is Interferon alpha (IFNα), more preferably pegylated Interferon alpha, which may be admixed to the medicament according to the invention, or may be administered separately, for example by subcutaneous injection to the subject. When administered separately the Interferon alpha is preferably also administered subcutaneously and is preferably administered at a dose of 1 microgram/kilogram of body weight within 10 cm proximity to the site where the medicament according to the invention is administered, such described in Zeestraten et al, 2013.

Another typical advantage of the medicaments according to the invention is that relatively low amounts of peptides may be used, in one single shot, in a simple formulation and without any adjuvant known to give undesired side-effects as Montanide ISA-51.

The medicament for intradermal administration may be any medicament according to the invention as defined herein. A medicament according to the invention used for subcutaneous administration may be the same as the one used for intradermal administration and may thus be any medicament according to the invention as defined herein. The skilled person knows how to formulate a medicament suited for subcutaneous administration.

Preferably, a medicament according to the invention for subcutaneous administration comprises a peptide as already herein defined in combination with an adjuvant. Preferred adjuvants or immune modulators have already been mentioned herein. Other preferred adjuvants are of the type of an oil-in water emulsions such as incomplete Freund's adjuvant or IFA, Montanide ISA-51 or Montanide ISA 720 (Seppic France). In a further preferred embodiment, a medicament according to the invention suited for subcutaneous administration comprises one or more peptides according to the invention, an adjuvant or immune modulator as earlier defined herein and an inert pharmaceutically acceptable carrier and/or excipients all as earlier defined herein. Formulation of medicaments, and the use of pharmaceutically acceptable excipients are known and customary in the art and for instance described in Remington; The Science and Practice of Pharmacy, 21^(st) Edition 2005, University of Sciences in Philadelphia. A preferred immune response stimulating compound or adjuvant for subcutaneous administration is Interferon alpha (IFNα), more preferably pegylated Interferon alpha, which may be admixed to the medicament according to the invention, or may be administered separately to the subject. When administered separately, the Interferon alpha is preferably also administered subcutaneously and is preferably administered at a dose of 1 microgram/kilogram of body weight within 10 cm proximity to the site where the medicament according to the invention is administered, such described in Zeestraten et al., 2013.

In an embodiment, the medicament according to the invention suited for intradermal administration may be simultaneously administered with a medicament according to the invention suited for subcutaneous administration. Alternatively, both medicaments may be sequentially intradermally and subsequently subcutaneously administered or vice versa (first subcutaneous administration followed by intradermal administration). In this embodiment as in the earlier described embodiment dedicated to the intradermal administration, the intradermal and/or subcutaneous administration of a medicament according to the invention, preferably a peptide according to the invention, and/or of an adjuvant may be repeated if needed and/or of distinct medicament, preferably peptides and/or of distinct adjuvants may be sequentially intradermally and/or subcutaneously administered. It is further encompassed by the present invention that a medicament according to the invention, preferably a peptide is administered intradermally and/or subcutaneously whereas an adjuvant as defined herein is sequentially administered as immune-modulator. The adjuvant or immune-modulator may be intradermally and/or subcutaneously administered. However any other way of administration may be used for the adjuvant or immune-modulator.

We expect the combination of an intradermal and a subcutaneous administration of a medicament according to the invention is advantageous. DC in the epidermis are clearly different from DC in the dermis and in the subcutis. The intracutaneous (intradermal) immunization will cause antigen processing and activation of epidermal DC (Langerin-positive Langerhans cells) that through their dendritic network are in close contact with the keratinocytes. This will also optimally activate inflammatory pathways in the interactions between Langerhans cell and keratinocytes, followed by trafficking of antigen loaded and activated Langerhans cell to the skin-draining lymph nodes. The subcutaneous administration will activate other DC subsets, that will also become loaded with antigen and travel independently to the skin-draining lymph nodes. Conceivably, the use of a medicament which may be administered both intradermally and subcutaneously may lead to a synergistic stimulation of T-cells in these draining nodes by the different DC subsets.

A medicament according to the present invention and the methods of treatment described herein using a medicament according to the invention may advantageously be combined with other medicaments and methods of treatment. As such, a medicament according to the invention or a method of treatment according to the invention may be combined with e.g. therapy, and/or antibody therapy against an HBV related disease or may be combined with e.g. immunotherapy and/or antibody therapy against another than HBV related disease, or may be combined with immunotherapy against another antigen than HBV to treat an HBV related disease.

In this document and in its claims, the verb “to comprise” and its conjugations is used in its non-limiting sense to mean that items following the word are included, but items not specifically mentioned are not excluded. In addition, reference to an element by the indefinite article “a” or “an” does not exclude the possibility that more than one of the element is present, unless the context clearly requires that there be one and only one of the elements. The indefinite article “a” or “an” thus usually means “at least one”. The word “about” or “approximately” when used in association with a numerical value (e.g. about 10) preferably means that the value may be the given value (of 10) more or less 0.1% of the value.

The sequence information as provided herein should not be so narrowly construed as to require inclusion of erroneously identified bases. The skilled person is capable of identifying such erroneously identified bases and knows how to correct for such errors. In case of sequence errors, the sequence of the HBV core, HBV polymerase and HBV large surface protein polypeptides obtainable by expression of the gene present in SEQ ID NO: 5, 2 and 1467 containing the respective nucleic acid sequence coding for the polypeptides should prevail.

All patent and literature references cited in the present specification are hereby incorporated by reference in their entirety.

Unless stated otherwise, the practice of the invention will employ standard conventional methods of molecular biology, virology, microbiology or biochemistry. Such techniques are described in Sambrook et al. (1989) Molecular Cloning, A Laboratory Manual (2^(nd) edition), Cold Spring Harbor Laboratory, Cold Spring Harbor Laboratory Press; in Sambrook and Russell (2001) Molecular Cloning: A Laboratory Manual, Third Edition, Cold Spring Harbor Laboratory Press, NY; in Volumes 1 and 2 of Ausubel et al. (1994) Current Protocols in Molecular Biology, Current Protocols, USA; and in Volumes I and II of Brown (1998) Molecular Biology LabFax, Second Edition, Academic Press (UK); Oligonucleotide Synthesis (N. Gait editor); Nucleic Acid Hybridization (Hames and Higgins, eds.).

BRIEF DESCRIPTION OF THE DRAWINGS

FIG. 1: Proteasome-mediated cleavage pattern of long vaccine peptides as predicted in silico and observed in experimental in vitro digestions. For each SLP, the observed cleavage sites are indicated by arrows (major and minor cleavage sites are indicated by bold and thin arrows, respectively, as further detailed herein). Further, for each of the ten SLPs tested in the digestion experiments (SLP1, SLP10 and SLP21 in FIG. 1A; SLP14, SLP18 and SLP21 in FIG. 1B; SLP24, SLP25 and SLP26 in FIG. 1C; and SLP 27 in FIG. 1D), the predicted C-score is indicated in the first row, the confirmed predicted cleavage sites are indicated in the second row (indicated as ‘+’), the amino acid position within the source protein is indicated in the third row, the respective amino acids in the sequence are indicated in the fourth row, and the amino acid number within the SLP is indicated in the fifth row. For SLP27, C* indicates the cysteine replacement by Abu.

FIG. 2: Overview of responding naïve donors after T cell induction with HBV-derived long peptides. Combined data of IFNγ production as measured by ELISA (‘ELISA’); hatched box SI (Stimulation Index)>1.5, and T cell proliferation (Profit) as measured by 3H thymidine incorporation; hatched box SI>1.5. N.t.: not tested

FIG. 3: Overview of responding HBV-immune donors after stimulation with HBV-derived long peptides. Data represent IFNγ-ELISpot results, with hatched boxes indicating a positive response with SI (Stimulation Index)>3, white boxes SI<3.

FIG. 4: The average Stimulation Index (SI) for each peptide, as measured in an IFNγ ELISpot assay, plotted against the predicted TRIA score of the corresponding peptide. Abu-SLP27 is indicated (φ).

The invention is further explained in the following examples. These examples do not limit the scope of the invention, but merely serve to clarify the invention.

EXAMPLES

Introduction

In the current invention, we developed an optimal T cell inducing vaccine composition consisting of synthetic long peptides to treat chronically HBV-infected patients. A selection of 37 long peptides (Table 3; sequences ranging from 30 to 39 amino acids) was made encompassing the regions of the HBV Polymerase, Core protein, Surface Antigen and X-protein with the highest putative T cell immunity inducing capacity. To this end first putative HLA class I restricted cytotoxic T cell (CTL) epitopes and putative HLA class II restricted T helper epitopes were identified in these proteins using algorithms that predict HLA class I and II peptide binding and C-terminal generation by the proteasome of all HLA class I binding short peptides (with a length of a CTL epitope; 8-12 aa) contained in the HBV proteins. Numerical values were assigned to all putative CTL epitopes and T helper epitopes reflecting their immunogenicity quality. The quality of any CTL epitope was assessed using the so-called Class I-BCI score (Class I-Binding-Cleavage-Immunogenicity score), incorporating the combination of the HLA class I binding capacity of the epitope in conjunction with the likelihood of its C-terminal liberation from the source protein by the proteasome. Putative T helper epitopes were assessed using the so-called Class II-B score (Class II-Binding score) reflecting their binding capacity and thus predicted immunogenic quality. The combined cumulative value, i.e. the sum of the cumulative Class I-BCI score and the cumulative Class II-B score, was calculated for all possible long peptides, reflecting the cumulative quantity and quality of all CTL epitopes and T helper epitopes, and is expressed in the T cell Regional Immunogenicity Assessment (TRIA) score. Accordingly, the TRIA score enabled the assessment of the total T cell immunogenicity of any possible long peptide (length 30-39 aa) in the HBV proteins. The 37 HBV-derived long peptides with the highest TRIA scores were selected. Next, we assessed whether naïve donors and donors that have cleared an HBV infection in the past are able to respond to one or more of a subset of 13 long peptides with varying TRIA scores selected from the broad set of 37 long peptides.

PBMC were obtained from buffy coats of twelve healthy donors, six of which were HBV-naïve and six others had cleared an HBV-infection in the past. Using long-term T cell induction assays, we found responses against 12 out of 13 peptides in naïve donors (eleven of which induced responses in multiple donors), confirming the ability of these SLPs to induce T cell responses in a great majority of individuals that had not encountered the antigens before. The strength of T cell responses found in PBMC of HBV-immune donors against these 13 long vaccine peptides correlated with their predicted strength of overall T cell immunogenicity, as expressed in their TRIA scores, validating the predictive value of the TRIA score for selecting immunogenic peptides. Thus the TRIA score is a reliable criterion for the selection of optimal immunogenic long peptides, invigorating us to select the long peptides with the highest TRIA scores into our HBV SLP-based vaccine.

Material and Methods

Peptide Synthesis

Peptides were synthesized using solid phase Fmoc/tBu chemistry on a PTI Prelude peptide synthesizer and purified on a Gilson preparative HPLC system to >95% purity. The identity and purity of the peptides were confirmed with UPLC-MS on a Waters Acquity UPLC/TQD system.

Prediction of CTL and T Helper Cell Immunity Inducing Capacity in Selected HBV-Derived SLPs by Net-Based Algorithm

The putative CTL immunity inducing capacity per SLP was predicted by calculating the cumulative Class I-BCI score per SLP. As detailed below, the cumulative BCI score is based on the Class I-B score, which is a measure for HLA class I peptide binding, and the C-score, which is a measure for proteosomal epitope liberation.

The putative T helper cell immunity inducing capacity per SLP was predicted by calculating the cumulative Class II-B score per SLP. As detailed below, the cumulative Class II-B score is based on the Class II-B score, which is a measure for HLA class II peptide binding.

The total putative immunity inducing capacity per SLP was predicted by summation of the cumulative Class I-BCI score and the cumulative Class II-B score, which value is denominated herein as the TRIA score.

Class I-B Score

Peptide binding to 50 HLA class I molecules (see text) of HBV polymerase-derived peptides, HBV Core protein-derived peptides, HBV Surface Antigen-derived peptides and HBV X protein-derived peptides was assessed in silico using a proprietary algorithm. The upper 1.5^(th) percentile of the predicted binding peptides to each HLA class I molecule was selected. The ‘Class I-Binding score (Class I-B score)’ is derived from the ranking of the predicted binding affinity of the peptides. Briefly, the ranking was first reversed and subsequently normalized to 100, so that the peptide predicted to bind best has a score of 100. Example: five peptides were selected (5 within the 1.5^(th) percentile). Peptides were first assigned the ‘reverse ranking score’ 5 to 1 (5 for the best binding peptide). Subsequently, each reverse ranking score is normalized to the number of peptides within the upper 1.5^(th) percentile, so that the best binder scores 100. To that end, the ranking score for each peptide is multiplied with 100/5 (=20). The best binder then obtains a Class I-B score: 5×20=100, the second best binder has a Class I-B score of 4×20=80, etc. In general, the ranking score is multiplied with 100/n (n=number of peptide within the 1.5^(th) percentile). As a consequence, the best predicted binder (to a certain HLA class I molecule) always scores 100, irrespective of the precise number of peptides within the 1.5^(th) percentile that are selected.

C-Score

C-terminal generation by the proteasome of the upper 1.5^(th) percentile of predicted high affinity binding peptides of HBV polymerase, HBV Core protein, HBV Surface Antigen and HBV X-protein (for each HLA class I molecule) was assessed using two proprietary algorithms, which predict the likelihood of a proteasomal cleavage after a certain amino acid position in HBV polymerase, HBV Core protein, HBV Surface Antigen and HBV X-protein, respectively, and can score between 0 and 1, where a higher value represents a higher likelihood of cleavage after the amino acid. The value 0.5 may be used as an arbitrary threshold value: >0.5 the cleavage is likely to occur, and <0.5 the cleavage is likely to not occur. Accordingly, a value close to 1 indicates a high likelihood of cleavage after the specific residue. Because great differences between the predictions by both different algorithms occur, we developed the Cleavage score (C-score) that takes into account the prediction results of both proprietary algorithms. The C-score is the summation of the separate scores by both methods. Therefore, the C-score for each position in HBV polymerase is maximally (close to) 2, and minimally (close to) 0, where close to 2 reflects a very high likelihood by BOTH methods that the cleavage after the residue will be produced by the proteasome, and a C-score close to 1 is considered as an indifferent tendency for cleavage by the proteasome (as predicted on average by both network methods).

Class I-BCI Score

To incorporate in one quantitative measure both the Class I-B score and the C-score, which are the measures indicative for the likelihood that a peptide will bind with high affinity to HLA class I molecules and will be C-terminally produced, the Class I-Binding-Cleavage-Immunogenicity (Class I-BCI) score was developed. The Class I-BCI score is the Class I-B score multiplied by the C-score. As such the Class I-BCI can attain a maximal value of 200 (100×2) (arbitrary units).

Cumulative Class I-BCI Score

The cumulative Class I-BCI score for each long peptide according to the invention was used as (one of two) selection criterion to identify the peptides of the invention. The cumulative Class I-BCI score is a quantitative reflection of both the total number of CD8⁺ cytotoxic T cell epitopes that are contained in a long peptide according to the invention and their predicted quality, in terms of binding capacity and likelihood of intracellular generation by the proteasome, and is as such indicative for the CD8⁺ cytotoxic T cell-inducing power of each peptide according to the invention (its CD8⁺ T cell immunogenicity). A relatively high cumulative Class I-BCI score of a peptide according to the invention indicates a high CD8⁺ T cell immunogenicity.

Class II-B Score

Peptide binding to 13 prevalent HLA class II molecules of HBV polymerase-derived peptides, HBV Core protein-derived peptides, HBV Surface Antigen-derived peptides and HBV X protein-derived peptides was assessed in silico using a proprietary algorithm. The ‘Class II-Binding score’ (Class II-B score) is derived from the ranking of the predicted binding affinity of the peptides. Briefly, the ranking was first reversed and subsequently normalized to 100, so that the peptide predicted to bind best has a score of 100. To reduce the number of peptides in the list, all length variants of peptides predicted to bind to a particular HLA class II molecule with a lower predicted binding (lower Class II-B score) are discarded in the list.

Cumulative Class II-B Score

The cumulative Class II-B score for each long peptide according to the invention was used as the second selection criterion to identify the peptides of the invention. The cumulative Class II-B score is a quantitative reflection of both the total number of CD4⁺ T-helper cell epitopes that are contained in a long peptide according to the invention and their predicted quality, in terms of binding capacity, and is as such indicative for the CD4⁺ T cell-inducing power of each peptide according to the invention (its CD4⁺ T cell immunogenicity). A relatively high cumulative Class II-B score of a peptide according to the invention indicates a high CD4⁺ T cell immunogenicity

T Cell Regional Immunogenicity Assessment (TRIA) Score

The TRIA score for a particular peptide of the invention (SLP) is the sum of cumulative Class I-BCI score and the cumulative Class II-B score of that particular long peptide of the invention (SLP).

Proteasomal Digestion

Dithiotreitol (DTT; Sigma-Aldrich) was freshly dissolved in UPLC-grade water and added to a 2× concentrated proteasome digestion buffer (60 mM Trizma-base; pH 7.5; Sigma-Aldrich, 20 mM KCl; Sigma-Aldrich, 10 mM MgCl₂; Sigma-Aldrich, 10 mM NaCl; Sigma-Aldrich) to an end concentration DTT of 2 mM. Then, 130 μl UPLC-grade water was added to 3 reaction vials, along with 150 μl of the 2× concentrated proteasome digestion buffer containing 2 mM DTT, and 10 μl of the peptide to be tested (stock concentration 300 nmol/ml). After vortexing the vials, 10 μl of water was added to vial 1 (mock control digest), 1 μg (10 μl) of constitutive 20S-proteasome (stock 0.1 mg/ml; Enzo Life Sciences) to vial 2, and 1 μg (10 μl) of immune 20S-proteasome (stock 0.1 mg/ml; Enzo Life Sciences) to vial 3. A 50 μl sample for T=0 was taken directly after vortexing and 4 μl of Formic acid (Sigma-Aldrich) was added to stop the reaction. The reaction vials were vortexed and incubated at 37° C. Samples of 50 μl were collected after 1 h, 3 h, 6 h and 24 h incubation. The reactions were stopped with 4 μl Formic acid, and all samples were stored at 20° C.

Mass Spectrometry Analysis of Digested Fragments

A Q-TOF1 mass spectrometer (Waters) equipped with an online nanoelectrospray interface with an approximate flow rate of 250 nl/min was used for electrospray ionization-mass spectrometry. Peptide-digestion samples were trapped on a precolumn (MCA-300-05-C18; Dionex) and were eluted with a steep gradient of 70-90% buffer B over 10 min (buffer A, water, acetonitrile and formic acid, 95:3:1 (vol/vol/vol); buffer B, water, acetonitrile and formic acid, 10:90:1 (vol/vol/vol)). Mass spectra were recorded from a mass of 50-2000 daltons. In tandem mass spectrometry mode, ions were selected with a window of 3 daltons. The collision gas was argon (4×10⁻⁵ mbar), and the collision voltage was ˜30 V. For peptide digestion by purified constitutive proteasome and immunoproteasome, peaks in the mass spectra were searched in source substrate peptides with BioLynx software (Waters) and the abundance of a specific digestion fragment was assessed quantitatively as its percentage of the total summed intensities, including undigested substrate.

Cells

Peripheral blood mononuclear cells (PBMC) from healthy donors were isolated by centrifugation over a Ficoll gradient. To generate dendritic cells (DCs), approximately 50*10⁶ PBMC were brought to a concentration of 3*10⁶ cells/ml complete medium (IMDM, Lonza, supplemented with 8% HS, Seralab; penicillin/streptomycin, Lonza; L-glutamin, Lonza) and seeded 3 ml/well in a 6-wells plate (Corning). After incubation for 1.5 hours at 37° C., non-adherent cells were washed away in three washing steps using complete medium (day 0). The adherent cells were cultured for three days at 37° C. in 2 ml/well of complete medium containing 800 U/ml GM-CSF and 500 U/ml IL-4 (Peprotech). On day 3, 1 ml of complete medium containing 2400 U/ml GM-CSF and 1500 U/ml IL-4 was added to each well and cultured for another three days at 37° C.

Induction of T Cells

On day 6, long peptides distributed over 3 pools were added to monocyte-derived DCs of naïve donors at a 3 nmol/ml concentration and incubated overnight at 37° C. Pool 1 comprises SLP 26 (SEQ ID NO: 76), SLP 24 (SEQ ID NO: 74), SLP 1 (SEQ ID NO: 51) and SLP 30 (SEQ ID NO: 1142); Pool 2 comprises Abu-SLP 27 (SEQ ID NO: 77, wherein the cysteine on amino acid position 1 is replaced by Abu), SLP 25 (SEQ ID NO: 75), SLP 10 (SEQ ID NO: 60) and SLP 34 (SEQ ID NO: 1469); and Pool 3 comprises SLP 5 (SEQ ID NO: 55), SLP 13 (SEQ ID NO: 63), SLP 14 (SEQ ID NO: 64) and SLP 21 (SEQ ID NO: 21). On day 7, the cells were washed twice with complete medium to remove peptides. DC and autologous PBMC were co-cultured in a 1:10 ratio for 10 days at 37° C. in the presence of 10 ng/ml IL-7 and 100 pg/ml IL-12p70. The T cell lines generated by this process were checked every 2-3 days and split when necessary.

Restimulation of T Cell Lines

Three days after T cell induction (day 10), a second batch of autologous DC was differentiated and loaded with peptide pools as described above. On day 10 after initiation of the T cell line (day 17), the peptide-loaded DC were washed twice with complete medium and added to the T cells in a 1:10 (DC:T cell) ratio in the presence of 10 ng/ml IL-7 and 100 pg/ml IL-12p70. The cells were co-cultured for 7 days. On day 17, also a new batch of DC was differentiated and loaded with peptide pools as described above. For this second restimulation, starting on day 24, DC and T cells were co-cultured in a 1:10 ratio. Two days after restimulation, 30 IU/ml IL-2 (Peprotech) and 5 ng/ml IL-15 (Peprotech) were added to the culture medium. A third restimulation, starting on day 31, was performed identically to the second restimulation.

T Cell Proliferation and IFNγ Production

To measure T cell activation and proliferation, autologous DC were loaded for 6 hours with each of the 13 HBV-derived peptides separately on day 23, 30 and 37 of the T cell induction protocol described above. The DCs were washed and 5,000 peptide-loaded DC were co-cultured with 50,000 T cells for 48 hours. Then, supernatant was collected for ELISA (IFNγ ELISA, Diaclone) and culture medium containing ³H thymidine was added to all wells. Radioactive ³H thymidine is incorporated in the DNA of newly formed (proliferated) cells, which is measured after 16 hours of incubation on a MicroBeta liquid scintillation counter (Wallac/Perkin Elmer).

IFNγ-ELISpot

To detect antigen-specific IFNγ-producing human T cells, the PBMC were first pre-stimulated with 3 nmol/ml of the indicated peptide for 72 hours at 37° C. During this stimulation, ELISpot PVDF plates (Mabtech) were coated with 5 ug/ml anti-human IFNγ mAb 1-D1K coating antibody (Mabtech) in PBS and incubated overnight at 4° C. After stimulation of the PBMC, the coating antibody was aspirated from the plate, and washed 4 times with PBS. To block aspecific binding, 100 μl of IMDM containing 8% FCS was added to all wells and incubated at 37° C. for 1 hour. In the meantime, stimulated PBMC were harvested, centrifuged, resuspended in X-vivo 15 medium (Lonza) and counted. All PBMC samples were brought to a concentration of 1.5*10⁶ cells/ml in X-vivo 15 medium. The medium in the wells of the PVDF plate was aspirated and 100 μl of each PBMC sample was added to the plate in quadruplicates. The plates were incubated at 37° C. overnight. The next day, the supernatant was discarded and plates are washed 6 times with PBS/Tween20 0.05%. The biotinylated anti-human IFNγ mAb 7-B6-1 (Mabtech) was added to all wells (100 μl/well) at a 0.3 μg/ml concentration in PBS with 1% FBS, and incubated for 2 hours at RT. Next, plates were washed 6 times using PBS/Tween20 0.05% and 1 μg/ml Extravidin-Alkaline phosphatase (ALP) (Sigma-Aldrich) was added to all wells (100 μl/well) in PBS with 1% FBS. The plates were incubated for 1 hour at RT. ALP substrate solution BCIP/NBT-plus (Mabtech) was prepared and 100 μl/well was added to all wells after the plates were washed 4 times with PBS/Tween20 0.05%. To terminate the colorimetric reaction (after 1-20 minutes), tap water was used to wash the plates extensively. After drying, the formed spots were measured on a Biosys Bioreader 5000.

Results

Selection of Long Peptides Based on HLA Class I Peptide Binding Prediction and Predicted C-Terminal Generation of all Possible CD8⁺ T Cell Epitopes Contained in the Long Peptides

A high quality CD8⁺ T cell epitope is defined as a peptide that possesses both a predicted high affinity for the HLA class I molecule to which it binds and is also predicted to be generated at its C-terminus by a proteolytic cleavage of the proteasome. Peptides according to the present invention were selected in HBV protein regions that contain optimally high numbers of high quality CD8⁺ and CD4⁺ T cell epitopes. To this end, first the HLA class I binding and C-terminal generation of all possible CD8⁺ T cell epitopes was assessed using a proprietary HLA class I peptide binding algorithm and two proprietary algorithms predicting the cleavages by the proteasome. Subsequently, we devised a single quantitative measure, the so-called binding-cleavage-immunogenicity (BCI) Class I-score, that for each short peptide (8-13 amino acids) incorporates both its predicted binding affinity for the HLA class I molecule to which it binds and the likelihood that the peptide is generated by the proteasome in the cells. The Class I-BCI score is calculated from (1) the binding Class I-score (Class I-B score), which is derived from the results of the in silico prediction of HLA class I peptide binding using the aforementioned algorithm, and (2) the cleavage score (C-score), which is derived from the results of the in silico prediction of the proteasome-mediated C-terminal generation of the peptide by the proteasome using the aforementioned algorithms. Tables 4a, 5a, 6a, and 7a present the Class I-BCI score for all possible CD8⁺ T cell epitopes of these Polymerase, Core protein, Surface Antigen or X-protein derived SLPs, respectively, together with the cumulative BCI Class I score. Tables 4b, 5b, 6b and 7b present the Class II-B score for all possible CD4⁺ T cell epitopes of these Polymerase, Core protein, Surface Antigen or X-protein derived SLPs, respectively, together with the cumulative Class II-B score. Together the cumulative Class I-BCI score (for CTL epitopes) and the cumulative B Class II-score (for T helper epitopes) resulted in one quantitative value, the so-called Total Regional Immunogenicity Assessment (TRIA) score, reflecting the overall T cell immunogenicity of a long vaccine peptide (Table 3). Based on the highest TRIA scores, 37 SLPs derived from HBV Polymerase, Core protein, Surface Antigen or X-protein were selected for further evaluation (Table 3). From these, to validate the predictive power of the TRIA score, we chose a representative set of 13 SLPs, which included SLP with relatively low and high TRIA scores, for in vitro immunogenicity assessment. These 13 peptides were divided over three peptide pools for T cell induction assays, as described (see below).

Peptide Fragment Analysis after Proteasomal Digestion of SLPs Reveals High Accuracy of in Silico Predictions

An important component of the identification of putative CTL epitopes is the prediction of their C-terminal generation by a proteasome-mediated cleavage. To validate the reliability of this prediction, proteasomal digestion patterns were experimentally assessed for all but 3 of the 13 functionally tested long vaccine peptides (three long peptides were not being cleaved due to technical reasons).

Digestion experiments were performed separately with 20S constitutive proteasomes and 20S immuno proteasome preparations. The combined analysis of cleavages produced by both types of proteasomes allows the assessment of the C-terminal generation of CTL epitopes that are expressed both on the surface of antigen presenting cells (mainly dendritic cells), containing immunoproteasomes, and on the surface of cancer cells, especially from solid tumors, which mainly express constitutive proteasomes. For vaccination purposes these epitopes are preferred because vaccination with such epitopes will allow the induction of CTL by vaccination and the subsequent eradication of cancer cells by these CTL after recognition of the epitopes on the surface of cancer cells.

As indicated in FIG. 1, 10 long peptides of the invention (length 30-39 aa) were co-incubated in an appropriate buffer with the proteasome preparations at 37° C. for 0, 1, 3, 6 and 24 h. After incubation for the indicated interval reactions were stopped and digestion mixtures, containing the digestion fragments, were measured by mass spectrometry as described herein. The mass spectra were (semi-quantitatively) analyzed to assess the position and abundance of the cleavage sites. The results of 24 h digestion are shown in FIG. 1.

The observed cleavage sites observed after 24 h incubation are indicated with arrows. Only cleavage sites that were observed in both the digestion with constitutive proteasomes and the digestion with immunoproteasomes are shown. Major cleavage sites and minor cleavages sites at 24 h digestion are depicted with bold and thin arrows, respectively, according to the following classification:

Major cleavage site: fragments containing as COOH terminus the residue NH₂-terminal from the cleavage site together with the (possible) complementary fragment(s) are present for ≥7% at 24 h incubation, as calculated from the intensities of the fragment peaks in the mass spectra. Minor cleavage site: fragments containing as COOH terminus the residue NH₂-terminal from the cleavage site together with the (possible) complementary fragment(s) are present for <7% at 24 h incubation. Cleavage sites with a cumulative fragment abundance of <1% are not shown.

FIG. 1 also indicates the C-score of proteasomal cleavage prediction. This score indicates the likelihood of cleavage C-terminal of the residue directly under the C-score. If the C-score>1 the cleavage site is considered predicted to be cleaved by both the constitutive proteasome and the immunoproteasome. As described herein, the C-score is a summation of the predictions by two in silico algorithms separately predicting the proteasome-mediated cleavages by constitutive proteasomes and the cleavages by immunoproteasomes. Each separate prediction can attain a maximal value of 1. Accordingly, the maximal value of the C-score is 2. C-scores>1 are together counted as the total number of predicted cleavage sites (the C-terminus of the long substrate peptide is not taken into account, because cleavage after this residue cannot be tested).

FIG. 1 further indicates the confirmed cleavages (indicated by ‘+’), which are those predicted cleavage sites (C-score>1) that are confirmed to be cleaved after 24 h in the proteasome-mediated digestion assay.

As indicated by FIG. 1, for SLP1 36% (4/11), for SLP10 71% (10/14), for SLP13 62% (10/16), for SLP14 100% (13/13), for SLP18 65% (13/20), for SLP21 87% (14/16), for SLP24 62% (10/16), for SLP25 57% (8/14), for SLP26 72% (8/11), and for SLP27 75% (9/12) of the predicted cleavage sites have been confirmed here.

Induction of T Cell Responses Against 12 Out of 13 Selected Peptides in a Naïve Population

To assess whether the 13 selected peptides are able to induce a T cell response in naïve donors, PBMC were isolated from buffy coats derived from six healthy donors that had not experienced an HBV-infection. These PBMC were restimulated with either of the 3 peptide pools to obtain T cell lines, that were subsequently stimulated with the selected 13 peptides. The production of IFNγ and T cell proliferation (³H thymidine incorporation) were measured as a read-out for T cell activation. Results are shown in FIG. 2, indicating the percentage of donors showing a positive T cell response with a stimulation index (SI) of 1.5 or higher. The SI is calculated by dividing the measured sample value by the value of non-stimulated control cells. Induced responses in naïve donors were detected against 12 of the 13 pre-selected peptides, while 11 pre-selected peptides induced a response in multiple naïve donors.

Strength of Pre-Existing T Cell Responses in HBV-Immune Donors Correlates with TRIA Score

Subjects that have gone through an HBV infection and successfully cleared it, possess circulating memory T cells specific for HBV. To assess the relevance of the selected vaccine peptides for the clearance of a naturally occurring HBV infection, we tested the presence of T cell responses against the 13 selected HBV peptides in PBMC derived from six HBV-immune donors. After isolation of the PBMC, cells were stimulated with each of the 13 peptides and an IFNγ-ELISpot was performed to detect T cell responses. PBMC samples from 3 out of 6 tested donors showed a positive IFNγ response against one or more of the 13 peptides (SI>3). Responses were observed against 11 (SLP 5, 10, 13, 14, 18, 21, 24, 25, 26, 27 and 34, represented by SEQ ID NO: 55, 60, 63, 64, 68, 71, 74, 75, 76, 77 and 1469, respectively) out of the 13 peptides, 6 of which induced responses in multiple donors (SLP 10, 13, 21, 24, 25 and 34, represented by SEQ ID NO: 60, 63, 71, 74, 75 and 1469, respectively). The results are summarized in FIG. 3, indicating the donors showing a positive IFNγ⁺ T cell response against a peptide. For each SLP tested, the average SI of the IFNγ-responses was calculated; 1.21 for SLP1, 2.11 for SLP5, 2.40 for SLP10, 2.44 for SLP13, 1.97 for SLP14, 1.86 for SLP18, 2.87 for SLP21, 2.54 for SLP24, 2.66 for SLP25, 1.56 for SLP26, 1.66 for Abu-SLP27, 1.49 for SLP30 and 3.02 for SLP34. Importantly, when the average SI of the IFNγ-responses to each peptide is plotted against the corresponding TRIA score, we see a significant correlation (FIG. 4), both while including (R²=0.37, p=0.028; see FIG. 4) the results of Abu-SLP27 and while excluding (R²=0.34, p=0.048; not shown) the results of Abu-SLP27. This validates the use of the TRIA score for the selection of immunogenic peptides.

Discussion

The experimental results presented herein validate, and therefore support, the selection and underscore the immunological relevance of the HBV-derived long vaccine peptides of the present invention. These long vaccine peptides encompass the HBV protein regions with the highest number of high quality HLA class I and HLA class II binding epitopes in an outbred population. A preferred combination of the vaccine peptides will be incorporated in a novel HBV SLP vaccine composition to treat chronically HBV-infected patients. Using algorithms to predict the peptide binding affinity of short peptides (8-12 aa) for all prevalent HLA class I molecules and the likelihood of the C-terminal generation of these short peptides by cleavage by the proteasome, in combination with the identification of the putative T helper epitopes, we identified highly immunogenic regions from which the optimal 37 long vaccine peptides were selected.

To enable proper selection of long vaccine peptides in the present invention, a quantitative measure was developed, the TRIA score. Without such a quantitative measure attributed to all possible long HBV peptides, a proper selection of the optimal long peptides is not possible. The TRIA score is a quantitative representation of the quality and quantity of all putative HLA class I restricted CD8⁺ cytotoxic T cell epitopes and HLA class II restricted CD4⁺ T helper epitopes contained in a long peptide. The TRIA score was calculated for all possible HBV peptides with a length of 30-39 aa, which is the optimal peptide length for vaccination purposes, enabling the rational selection of a set of highly immunogenic long vaccine peptides.

For further testing and validation of the immunological relevance, we selected a set of 13 SLP with varying TRIA scores. First, we experimentally digested these SLP using either constitutive proteasome or immunoproteasome. The generated fragments showed a clear overlap with the predicted C-terminal cleavage sites, expressed in the BCI score.

Thereafter, T cell assays were performed using PBMC from both naïve and HBV-immune donors. Nearly all 13 selected SLPs were able to induce T cell responses in PBMC derived from naïve healthy donors, which proves that the selected SLP set has the potential to induce responses by the T cell repertoire that had not been stimulated before. Within the same set of vaccine peptides, a strong correlation was observed between the TRIA score of a certain vaccine peptide and the strength of the IFNγ-response in HBV-immune donors, indicating that the TRIA score is a predictive value for in vivo immunogenicity and thus functionality of the vaccine peptides.

TABLE 1 Protein and DNA sequences of HBV polymerase, HBV core and HBV large surface proteins. SEQ ID Gene/Gene NO: SEQ type product Sequence    1 Protein HBV MPLSYQHFRKLLLLDDGTEAGPLEEELPRLADADLHRRVAE Polymerase DLNLGNLNVSIPWTHKVGNFTGLYSSTVPIFNPEWQTPSFP KIHLQEDIINRCQQFVGPLTVNEKRRLKLIMPARFYPTHTK YLPLDKGIKPYYPDQVVNHYFQTRHYLHTLWKAGILYKRET TRSASFCGSPYSWEQELQHGRLVIKTSQRHGDESFCSQSSG ILSRSSVGPCIRSQLKQSRLGLQPRQGRLASSQPSRSGSIR AKAHPSTRRYFGVEPSGSGHIDHSVNNSSSCLHQSAVRKAA YSHLSTSKRQSSSGHAVEFHCLPPNSAGSQSQGSVSSCWWL QFRNSKPCSEYCLSHLVNLREDWGPCDEHGEHHIRIPRTPA RVTGGVFLVDKNPHNTAESRLVVDFSQFSRGISRVSWPKFA VPNLQSLTNLLSSNLSWLSLDVSAAFYHIPLHPAAMPHLLI GSSGLSRYVARLSSNSRINNNQYGTMQNLHDSCSRQLYVSL MLLYKTYGWKLHLYSHPIVLGFRKIPMGVGLSPFLLAQFTS AICSVVRRAFPHCLAFSYMDDVVLGAKSVQHRESLYTAVTN FLLSLGTHLNPNKTKRWGYSLNFMGYIIGSWGTLPQDHIVQ KIKHCFRKLPVNRPIDWKVCQRIVGLLGFAAPFTQCGYPAL MPLYACIQAKQAFTFSPTYKAFLSKQYMNLYPVARQRPGLC QVFADATPTGWGLAIGHQRMRGTFVAPLPIHTAELLAACFA RSRSGAKLIGTDNSVVLSRKYTSFPWLLGCTANWILRGTSF VYVPSALNPADDPSRGRLGLSRPLLRLPFQPTTGRTSLYAV SPSVPSHLPVRVHFASPLHVAWRPP    2 CDS HBV See sequence listing Polymerase    3 Genomic HBV genome See sequence listing    4 Protein HBV Core MQLFHLCLIISCTCPTVQASKLCLGWLWGMDIDPYKEFGAT VELLSFLPSDFFPSVRDLLDTASALYREALESPEHCSPHHT ALRQAILCWGELMTLATWVGNNLEDPASRDLVVNYVNTNVG LKIRQLLWFHISCLTFGRETVLEYLVSFGVWIRTPPAYRPP NAPILSTLPETTVVRRRDRGRSPRRRTPSPRRRRSPSPRRR RSQSRESQC    5 CDS HBV Core See sequence listing 1141 Protein HBV MGGWSSKPRKGMGTNLSVPNPLGFFPDHQLDPAFGANSNNP large surface DWDFNPVKDDWPAANQVGVGAFGPRLTPPHGGILGWSPQAQ protein GILTTVSTIPPPASTNRQSGRQPTPISPPLRDSHPQAMQWN STAFHQTLQDPRVRGLYLPAGGSSSGTVNPAPNIASHISSI SARTGDPVTNMENITSGFLGPLLVLQAGFFLLTRILTIPQS LDSWWTSLNFLGGSPVCLGQNSQSPTSNHSPTSCPPICPGY RWMCLRRFITFLFILLLCLIFLLVLLDYQGMLPVCPLIPGS TTTSTGPCKTCTTPAQGNSMFPSCCCTKPTDGNCTCIPIPS SWAFAKYLWEWASVRFSWLSLLVPFVQWFVGLSPTVWLSAI WMMWYWGPSLYSIVSPFIPLLPIFFCLWVYI

TABLE 2 Different HBV X protein variants and the deduced consensus protein sequence. Number of mismatches as compared SEQ ID UniProt to consensus NO. ENTRY HBV genotype source sequence X protein sequence  6 Q916C38 Hepatitis B virus genotype A1 subtype adw2 (isolate South Africa/84/2001) (HBV-A) 12 see sequence listing  7 O91531 Hepatitis B virus genotype A2 (isolate Japan/11D11HCCW/1998) (HBV-A)  9 see sequence listing  8 P69714 Hepatitis B virus genotype A2 subtype adw (isolate Japan/Nishioka/1983) (HBV-A)  8 see sequence listing  9 P17102 Hepatitis B virus genotype A2 subtype adw2 (isolate Germany/991/1990) (HBV-A)  7 see sequence listing 10 P69713 Hepatitis B virus genotype A2 subtype adw2 (strain Rutter 1979) (HBV-A)  7 see sequence listing 11 Q4R1S1 Hepatitis B virus genotype A3 (isolate Cameroon/CMR711/1994) (HBV-A) 16 see sequence listing 12 Q4R159 Hepatitis B virus genotype A3 (isolate Cameroon/CM1R983/1994) (HBV-A) 15 see sequence listing 13 P00678 Hepatitis B virus genotype B1 (isolate Japan/Ry30/2002) (HBV-B) 11 see sequence listing 14 Q9PX75 Hepatitis B virus genotype B1 (isolate Japan/Yamagata-2/1998) (HBV-B) 12 see sequence listing 15 P20976 Hepatitis B virus genotype B1 subtype adw (isolate Japan/pJDW233/1988) (HBV-B)  8 see sequence listing 16 P20975 Hepatitis B virus genotype B2 (isolate Indonesia/p1DW420/1988) (HBV-B) 10 see sequence listing 17 Q9PXA2 Hepatitis B virus genotype B2 (isolate Vietnam/16091/1992) (HBV-B) 15 see sequence listing 18 P00685 Hepatitis B virus genotype B2 (isolate Vietnam/9873/1997) (HBV-B) 11 see sequence listing 19 Q67923 Hepatitis B virus genotype B2 subtype adw (isolate China/patient4/1996) (HBV-B) 11 see sequence listing 20 P20977 Hepatitis B virus genotype B/C subtype adw (isolate Okinawa/pODW282/1998) (HBV-B) 12 see sequence listing 21 Q9E658 Hepatitis B virus genotype C (isolate Vietnam/3270/2000) (HBV-C)  6 see sequence listing 22 P00686 Hepatitis B virus genotype C subtype adr (isolate Japan/Nishioka/1983) (HBV-C)  9 see sequence listing 23 P12936 Hepatitis B virus genotype C subtype adr (strain Japan/adr4/1983) (HBV-C)  8 see sequence listing 24 Q9YZR6 Hepatitis B virus genotype C subtype ar (isolate Japan/S-207/1988) (HBV-C) 10 see sequence listing 25 Q69027 Hepatitis B virus genotype C subtype ayr (isolate Human/Japan/Okamoto/-) (HBV-C)  8 see sequence listing 26 P00687 Hepatitis B virus genotype C subtype ayw (isolate Australia/AustRC/1992) (HBV-C) 14 see sequence listing 27 Q913A9 Hepatitis B virus genotype C subtype ayw (isolate China/Tibet127/2002) (HBV-C)  5 see sequence listing 28 P24026 Hepatitis B virus genotype D (isolate France/alphal/1989) (HBV-D) 12 see sequence listing 29 O93195 Hepatitis B virus genotype D (isolate Germany/1-91/1991) (HBV-D) 14 see sequence listing 30 POC681 Hepatitis B virus genotype D subtype ayw (isolate Australia/AustKW/1991) (HBV-D)  9 see sequence listing 31 P03165 Hepatitis B virus genotype D subtype ayw (isolate France/Tiollais/1979) (HBV-D)  7 see sequence listing 32 Q67877 Hepatitis B virus genotype D subtype ayw (isolate Italy/CI/1992) (HBV-D)  8 see sequence listing 33 Q9QMI3 Hepatitis B virus genotype D subtype ayw (isolate Japan/JYVV796/1988) (HBV-D)  9 see sequence listing 34 Q801U8 Hepatitis B virus genotype E (isolate Cote d'Ivoire/ABI-129/2003) (HBV-E) 11 see sequence listing 35 Q801U5 Hepatitis B virus genotype E (isolate Cote d'Ivoire/ABI-212/2003) (HBV-E)  7 see sequence listing 36 Q69604 Hepatitis B virus genotype E subtype ayw4 (isolate Kou) (HBV-E)  8 see sequence listing 37 Q8JMY3 Hepatitis B virus genotype F1 subtype adw4 (isolate El Salvador/1116Sal/1997) (HBV-F) 20 see sequence listing 38 Q99HR6 Hepatitis B virus genotype F2 (isolate Argentina/sal6/2000) (HBV-F) 19 see sequence listing 39 Q05499 Hepatitis B virus genotype F2 (isolate Brazil/w4B) (HBV-F) 21 see sequence listing 40 Q69607 Hepatitis B virus genotype F2 subtype adw4q (isolate Senegal/9203) (HBV-F) 21 see sequence listing 41 Q9IB15 Hepatitis B virus genotype G (isolate IG29227/2000) (HBV-G) 31 see sequence listing 42 Q8JMY5 Hepatitis B virus genotype H (isolate United States/LAS2523/2002) (HBV-H) 22 see sequence listing 43 Q8JNO6 Hepatitis B virus genotype H subtype adw4 (isolate Nicaragua/1853Nic/1997) (HBV-H) 22 see sequence listing 44 Q8JMZ5 Hepatitis B virus genotype H subtype adw4 (isolate Nicaragua/2928Nic/1997) (HBV-H) 22 see sequence listing 45 — Consensus aa sequence — MAARLCCQLDPARDVLCLRPV GAESRGRPLSGPLGALPSPSP SAVPADHGAHLSLRGLPVCAF SSAGPCALRFTSARRMETTVN AHQILPKVLHKRTLGLSAMST TDLEAYFKDCVFKDWEELGEE IRLKVFVLGGCRHKLVCSPAP CNFFTSA

TABLE 3 Synthetic long peptide (SLP) sequences. SEQ Cumulative Cumulative ID Class I- Class II-B TRIA NO: SLP # BCI ^(A) score^(B) score^(C) Source Sequence  51 SLP1  7264  780  8044 HBV Polymerase aa 1-30 MPLSYQHFRKLLLLDDGTEAGPLEEELPRL  52 SLP2  6943 1323  8266 HBV Polymerase aa 52-86 IPWTHKVGNFTGLYSSTVPIFNPEWQTPSFPKIHL  53 SLP3  6469 3070  9539 HBV Polymerase aa 103-135 VNEKRRLKLIMPARFYPTHTKYLPLDKGIKPYY  54 SLP4  6169  143  6312 HBV Polymerase aa 118-150 YPTHTKYLPLDKGIKPYYPDQVVNHYFQTRHYL  55 SLP5 11815 1519 13334 HBV Polymerase aa 139-177 VVNHYFQTRHYLHTLWKAGILYKRETTRSASFCGSPYSW  56 SLP6 10432  928 11360 HBV Polymerase aa 143-177 YFQTRHYLHTLWKAGILYKRETTRSASFCGSPYSW  57 SLP7 10325 1817 12142 HBV Polymerase aa 137-170 DQVVNHYFQTRHYLHTLWKAGILYKRETTRSASF  58 SLP8  7246    3  7249 HBV Polymerase aa 316-347 SQSQGSVSSCWWLQFRNSKPCSEYCLSHLVNL  59 SLP9  6722  527  7249 HBV Polymerase aa 385-417 TAESRLVVDFSQFSRGISRVSWPKFAVPNLQSL  60 SLP10 11926  943 12869 HBV Polymerase aa 419-456 NLLSSNLSWLSLDVSAAFYHIPLHPAAMPHLLIGSSGL  61 SLP11 12384 1058 13442 HBV Polymerase aa 422-459 SSNLSWLSLDVSAAFYHIPLHPAAMPHLLIGSSGLSRY  62 SLP12 12198  426 12624 HBV Polymerase aa 427-459 WLSLDVSAAFYHIPLHPAAMPHLLIGSSGLSRY  63 SLP13 15733 3046 18779 HBV Polymerase aa 481-514 HDSCSRQLYVSLMLLYKTYGWKLHLYSHPIVLGF  64 SLP14 12015 1042 13057 HBV Polymerase aa 524-559 SPFLLAQFTSAICSVVRRAFPHCLAFSYMDDVVLGA  65 SLP15 11658  783 12441 HBV Polymerase aa 526-559 FLLAQFTSAICSVVRRAFPHCLAFSYMDDVVLGA  66 SLP16  8255 1482  9737 HBV Polymerase aa 565-598 RESLYTAVTNFLLSLGIHLNPNKTKRWGYSLNFM  67 SLP17  6396  223  6619 HBV Polymerase aa 584-617 NPNKTKRWGYSLNFMGYIIGSWGTLPQDHIVQKI  68 SLP18 12576 1365 13941 HBV Polymerase aa 653-691 YPALMPLYACIQAKQAFTFSPTYKAFLSKQYMNLYPVAR  69 SLP19 10420 1181 11601 HBV Polymerase aa 657-691 MPLYACIQAKQAFTFSPTYKAFLSKQYMNLYPVAR  70 SLP20  7869  244  8113 HBV Polymerase aa 715-746 QRMRGTFVAPLPIHTAELLAACFARSRSGAKL  71 SLP21  8555 1591 10146 HBV Polymerase aa 754-791 VLSRKYTSFPWLLGCTANWILRGTSFVYVPSALNPADD  72 SLP22  6817 1709  8526 HBV Polymerase aa 757-792 RKYTSFPWLLGCTANWILRGTSFVYVPSALNPADDP  73 SLP23  8553  903  9456 HBV Polymerase aa 754-789 VLSRKYTSFPWLLGCTANWILRGTSFVYVPSALNPA  74 SLP24  7277 4649 11926 HBV Core aa 107-141 DPASRDLVVNYVNTNVGLKIRQLLWFHISCLTFGR  75 SLP25 11331 5493 16824 HBV Core aa 136-169 CLTFGRETVLEYLVSFGVWIRTPPAYRPPNAPIL  76 SLP26  5422 4414  9836 HBV consensus seq X protein aa 36-68 ALPSPSPSAVPADHGAHLSLRGLPVCAFSSAGP  77 SLP27  6468 3788 10256 HBV consensus seq X protein aa 61-95 CAFSSAGPCALRFTSARRMETTVNAHQILPKVLHK  78 SLP28  7354 3170 10524 HBV consensus seq X protein aa 86-120 HQILPKVLHKRTLGLSAMSTTDLEAYFKDCVFKDW  79 SLP29  5862 1024  6886 HBV consensus seq X protein aa 108-141 LEAYFKDCVFKDWEELGEEIRLKVFVLGGCRHKL 1142 SLP30  6882 4798 11680 HBV large surface protein aa 175-210 MENITSGFLGPLLVLQAGFFLLTRILTIPQSLDSWW 1143 SLP31 10214 7238 17452 HBV large surface protein aa 239-274 CPPICPGYRWMCLRRFIIFLFILLLCLIFLLVLLDY 1144 SLP32 14976 1815 16791 HBV large surface protein aa 323-358 CIPIPSSWAFAKYLWEWASVRFSWLSLLVPFVQWFV 1468 SLP33 13107 1815 14922 HBV large surface protein aa 327-358 PSSWAFAKYLWEWASVRFSWLSLLVPFVQWFV 1469 SLP34 12851 1815 14666 HBV large surface protein aa 328-358 SSWAFAKYLWEWASVRFSWLSLLVPFVQWFV 1145 SLP35  9736 4425 14161 HBV large surface protein aa 365-400 WLSAIWMMWYWGPSLYSIVSPFIPLLPIFFCLWVYI 1470 SLP36  5389 4035  9424 HBV large surface protein aa 371-400 MMWYWGPSLYSIVSPFIPLLPIFFCLWVYI 1471 SLP37  6880 4160 11040 HBV large surface protein aa 370-400 WMMWYWGPSLYSIVSPFIPLLPIFFCLWVYI ^(A) Cumulative Class I-BCI score: See Material and Methods (Examples section). ^(B)Cumulative Class II-B score: See Material and Methods (Examples section). ^(C)TRIA score is the sum of the Cumulative Class I-BCI score and the Cumulative Class II-B score.

TABLE 4a Predicted HLA class I-restricted CD8⁺ cytotoxic T cell epitopes contained in SLP sequences from HBV polymerase protein. HLA class I binding peptides in SLP sequences derived from HBV Polymerase protein Peptide of SEQ HLA Class invention (SLP) ID class I Class I-B I-BCI SLP SLP Start End Length Sequence^(A) NO: molecule score^(B) C-score^(C) score^(D) SLP# Start End 1 8 8 MPLSYQHF 80 A*6802 9 1,42 13 1 1 30 1 8 8 MPLSYQHF ″ B*0801 20 ″ 29 1 ″ ″ 1 8 8 MPLSYQHF ″ B*1402 62 ″ 88 1 ″ ″ 1 8 8 MPLSYQHF ″ B*1502 13 ″ 18 1 ″ ″ 1 8 8 MPLSYQHF ″ B*1801 57 ″ 81 1 ″ ″ 1 8 8 MPLSYQHF ″ B*3503 96 ″ 136 1 ″ ″ 1 8 8 MPLSYQHF ″ B*5101 77 ″ 109 1 ″ ″ 1 8 8 MPLSYQHF ″ B*5301 92 ″ 130 1 ″ ″ 1 8 8 MPLSYQHF ″ B*5501 26 ″ 36 1 ″ ″ 1 8 8 MPLSYQHF ″ B*5601 23 ″ 33 1 ″ ″ 1 9 9 MPLSYQHFR 81 A*3101 77 1,83 142 1 ″ ″ 1 9 9 MPLSYQHFR ″ A*3303 77 ″ 142 1 ″ ″ 1 9 9 MPLSYQHFR ″ A*6801 78 ″ 143 1 ″ ″ 1 9 9 MPLSYQHFR ″ B*5101 22 ″ 40 1 ″ ″ 2 9 8 PLSYQHFR 82 A*3101 22 ″ 39 1 ″ ″ 2 9 8 PLSYQHFR ″ A*3303 45 ″ 83 1 ″ ″ 2 9 8 PLSYQHFR ″ A*7401 28 ″ 51 1 ″ ″ 1 10 10 MPLSYQHFRK 83 B*3501 41 1,21 50 1 ″ ″ 3 10 8 LSYQHFRK 84 A*0301 90 ″ 110 1 ″ ″ 3 10 8 LSYQHFRK ″ A*1101 89 ″ 108 1 ″ ″ 3 10 8 LSYQHFRK ″ A*3001 43 ″ 53 1 ″ ″ 3 10 8 LSYQHFRK ″ A*7401 45 ″ 55 1 ″ ″ 1 11 11 MPLSYQHFRKL 85 B*0702 87 1,89 165 1 ″ ″ 1 11 11 MPLSYQHFRKL ″ B*0801 97 ″ 183 1 ″ ″ 1 11 11 MPLSYQHFRKL ″ B*1402 96 ″ 182 1 ″ ″ 1 11 11 MPLSYQHFRKL ″ B*3501 45 ″ 86 1 ″ ″ 1 11 11 MPLSYQHFRKL ″ B*3503 86 ″ 164 1 ″ ″ 1 11 11 MPLSYQHFRKL ″ B*3901 58 ″ 111 1 ″ ″ 1 11 11 MPLSYQHFRKL ″ B*5101 90 ″ 170 1 ″ ″ 1 11 11 MPLSYQHFRKL ″ B*5301 66 ″ 124 1 ″ ″ 1 11 11 MPLSYQHFRKL ″ B*5501 79 ″ 150 1 ″ ″ 1 11 11 MPLSYQHFRKL ″ B*5601 62 ″ 117 1 ″ ″ 3 11 9 LSYQHFRKL 86 B*5201 45 ″ 85 1 ″ ″ 4 11 8 SYQHFRKL 87 A*2301 57 ″ 108 1 ″ ″ 4 11 8 SYQHFRKL ″ A*2402 65 ″ 123 1 ″ ″ 3 12 10 LSYQHFRKLL 88 B*5201 37 1,82 68 1 ″ ″ 4 12 9 SYQHFRKLL 89 A*2402 26 ″ 48 1 ″ ″ 5 12 8 YQHFRKLL 90 B*0801 66 ″ 120 1 ″ ″ 5 12 8 YQHFRKLL ″ B*1402 54 ″ 98 1 ″ ″ 5 12 8 YQHFRKLL ″ B*3901 78 ″ 142 1 ″ ″ 5 12 8 YQHFRKLL ″ B*4801 71 ″ 130 1 ″ ″ 3 13 11 LSYQHFRKLLL 91 B*0801 59 1,71 101 1 ″ ″ 3 13 11 LSYQHFRKLLL ″ B*5201 65 ″ 111 1 ″ ″ 3 13 11 LSYQHFRKLLL ″ B*5701 11 ″ 18 1 ″ ″ 4 13 10 SYQHFRKLLL 92 A*2301 28 ″ 47 1 ″ ″ 4 13 10 SYQHFRKLLL ″ A*2402 33 ″ 57 1 ″ ″ 5 13 9 YQHFRKLLL 93 B*0801 31 ″ 52 1 ″ ″ 5 13 9 YQHFRKLLL ″ B*1402 61 ″ 104 1 ″ ″ 5 13 9 YQHFRKLLL ″ B*3901 64 ″ 109 1 ″ ″ 5 13 9 YQHFRKLLL ″ B*4801 98 ″ 168 1 ″ ″ 6 13 8 QHFRKLLL 94 B*1402 80 ″ 136 1 ″ ″ 6 13 8 QHFRKLLL ″ B*3801 55 ″ 94 1 ″ ″ 6 13 8 QHFRKLLL ″ B*3901 77 ″ 131 1 ″ ″ 4 14 11 SYQHFRKLLLL 95 A*2301 76 1,85 140 1 ″ ″ 4 14 11 SYQHFRKLLLL ″ A*2402 82 ″ 152 1 ″ ″ 5 14 10 YQHFRKLLLL 96 A*0201 36 ″ 67 1 ″ ″ 5 14 10 YQHFRKLLLL ″ B*1402 53 ″ 97 1 ″ ″ 5 14 10 YQHFRKLLLL ″ B*3901 70 ″ 130 1 ″ ″ 5 14 10 YQHFRKLLLL ″ B*4801 85 ″ 156 1 ″ ″ 6 14 9 QHFRKLLLL 97 B*1402 60 ″ 110 1 ″ ″ 6 14 9 QHFRKLLLL ″ B*3801 84 ″ 155 1 ″ ″ 7 14 8 HFRKLLLL 98 B*0801 75 ″ 138 1 ″ ″ 5 15 11 YQHFRKLLLLD 99 B*2705 94 0,80 75 1 ″ ″ 6 16 11 QHFRKLLLLDD 100 B*2705 18 0,57 10 1 ″ ″ 8 18 11 FRKLLLLDDGT 101 B*2705 51 0,12 6 1 ″ ″ 12 20 9 LLLDDGTEA 102 A*0201 24 1,41 34 1 ″ ″ 13 23 11 LLDDGTEAGPL 103 A*0206 33 0,79 26 1 ″ ″ 18 27 10 TEAGPLEEEL 104 B*1301 70 1,36 96 1 ″ ″ 18 27 10 TEAGPLEEEL ″ B*3701 10 ″ 13 1 ″ ″ 18 27 10 TEAGPLEEEL ″ B*3801 35 ″ 47 1 ″ ″ 18 27 10 TEAGPLEEEL ″ B*4002 60 ″ 82 1 ″ ″ 23 30 8 LEEELPRL 105 B*0702 75 1,77 133 1 ″ ″ 23 30 8 LEEELPRL ″ B*1301 69 ″ 122 1 ″ ″ 23 30 8 LEEELPRL ″ B*3701 52 ″ 93 1 ″ ″ 23 30 8 LEEELPRL ″ B*3801 33 ″ 58 1 ″ ″ 23 30 8 LEEELPRL ″ B*4001 74 ″ 131 1 ″ ″ Cumulative BCI Class I score^(E): 7264 52 61 10 IPWTHKVGNF 106 B*1402 43 1,19 52 2 52 86 52 61 10 IPWTHKVGNF ″ B*3501 47 ″ 55 2 ″ ″ 52 61 10 IPWTHKVGNF ″ B*3503 64 ″ 76 2 ″ ″ 52 61 10 IPWTHKVGNF ″ B*5301 41 ″ 49 2 ″ ″ 52 61 10 IPWTHKVGNF ″ B*5501 41 ″ 48 2 ″ ″ 54 61 8 WTHKVGNF 107 A*2501 84 ″ 100 2 ″ ″ 54 61 8 WTHKVGNF ″ A*2601 82 ″ 98 2 ″ ″ 54 61 8 WTHKVGNF ″ B*4601 44 ″ 53 2 ″ ″ 54 61 8 WTHKVGNF ″ B*5802 10 ″ 12 2 ″ ″ 52 62 11 IPWTHKVGNFT 108 B*5501 50 0,50 25 2 ″ ″ 52 62 11 IPWTHKVGNFT ″ B*5601 60 ″ 30 2 ″ ″ 54 64 11 WTHKVGNFTGL 109 A*2501 80 1,66 132 2 ″ ″ 54 64 11 WTHKVGNFTGL ″ A*2601 64 ″ 107 2 ″ ″ 56 64 9 HKVGNFTGL 110 B*1402 23 ″ 39 2 ″ ″ 56 64 9 HKVGNFTGL ″ B*3901 35 ″ 58 2 ″ ″ 57 64 8 KVGNFTGL 111 A*3201 32 ″ 53 2 ″ ″ 55 65 11 THKVGNFTGLY 112 A*3002 28 1,39 39 2 ″ ″ 56 65 10 HKVGNFTGLY 113 A*2601 23 ″ 32 2 ″ ″ 56 65 10 HKVGNFTGLY ″ A*2902 21 ″ 29 2 ″ ″ 56 65 10 HKVGNFTGLY ″ A*3002 80 ″ 111 2 ″ ″ 57 65 9 KVGNFTGLY 114 A*0101 34 ″ 47 2 ″ ″ 57 65 9 KVGNFTGLY ″ A*0301 39 ″ 55 2 ″ ″ 57 65 9 KVGNFTGLY ″ A*2902 79 ″ 110 2 ″ ″ 57 65 9 KVGNFTGLY ″ A*3002 100 ″ 139 2 ″ ″ 58 65 8 VGNFTGLY 115 A*0101 49 ″ 68 2 ″ ″ 58 65 8 VGNFTGLY ″ A*2902 62 ″ 86 2 ″ ″ 58 65 8 VGNFTGLY ″ A*3002 93 ″ 129 2 ″ ″ 61 71 11 FTGLYSSTVPI 116 A*2501 24 1,12 27 2 ″ ″ 61 71 11 FTGLYSSTVPI ″ A*3201 30 ″ 34 2 ″ ″ 61 71 11 FTGLYSSTVPI ″ A*6802 31 ″ 35 2 ″ ″ 61 71 11 FTGLYSSTVPI ″ B*5101 15 ″ 17 2 ″ ″ 61 71 11 FTGLYSSTVPI ″ B*5201 24 ″ 26 2 ″ ″ 62 71 10 TGLYSSTVPI 117 B*5201 33 ″ 37 2 ″ ″ 63 71 9 GLYSSTVPI 118 A*0201 69 ″ 77 2 ″ ″ 63 71 9 GLYSSTVPI ″ A*3201 88 ″ 99 2 ″ ″ 63 71 9 GLYSSTVPI ″ B*1525 42 ″ 48 2 ″ ″ 63 71 9 GLYSSTVPI ″ B*5201 35 ″ 40 2 ″ ″ 64 71 8 LYSSTVPI 119 A*2301 66 ″ 73 2 ″ ″ 64 71 8 LYSSTVPI ″ A*2402 81 ″ 91 2 ″ ″ 63 72 10 GLYSSTVPIF 120 A*2402 44 1,40 61 2 ″ ″ 63 72 10 GLYSSTVPIF ″ A*3001 74 ″ 104 2 ″ ″ 63 72 10 GLYSSTVPIF ″ B*1501 95 ″ 133 2 ″ ″ 63 72 10 GLYSSTVPIF ″ B*1502 80 ″ 112 2 ″ ″ 63 72 10 GLYSSTVPIF ″ B*1525 92 ″ 128 2 ″ ″ 64 72 9 LYSSTVPIF 121 A*2301 79 ″ 111 2 ″ ″ 64 72 9 LYSSTVPIF ″ A*2402 98 ″ 138 2 ″ ″ 65 72 8 YSSTVPIF 122 A*0101 26 ″ 37 2 ″ ″ 65 72 8 YSSTVPIF ″ B*4601 85 ″ 119 2 ″ ″ 65 72 8 YSSTVPIF ″ B*5301 59 ″ 83 2 ″ ″ 65 72 8 YSSTVPIF ″ B*5701 56 ″ 79 2 ″ ″ 65 72 8 YSSTVPIF ″ B*5801 80 ″ 112 2 ″ ″ 65 72 8 YSSTVPIF ″ B*5802 77 ″ 108 2 ″ ″ 65 74 10 YSSTVPIFNP 123 B*5701 98 0,65 64 2 ″ ″ 65 74 10 YSSTVPIFNP ″ B*5801 85 ″ 55 2 ″ ″ 66 76 11 SSTVPIFNPEW 124 B*5701 100 1,48 148 2 ″ ″ 66 76 11 SSTVPIFNPEW ″ B*5801 97 ″ 143 2 ″ ″ 66 76 11 SSTVPIFNPEW ″ B*5802 93 ″ 137 2 ″ ″ 67 76 10 STVPIFNPEW 125 B*4402 19 ″ 28 2 ″ ″ 67 76 10 STVPIFNPEW ″ B*4403 64 ″ 95 2 ″ ″ 67 76 10 STVPIFNPEW ″ B*5802 91 ″ 135 2 ″ ″ 69 76 8 VPIFNPEW 126 B*3503 5 ″ 8 2 ″ ″ 69 76 8 VPIFNPEW ″ B*5101 32 ″ 47 2 ″ ″ 69 76 8 VPIFNPEW ″ B*5301 90 ″ 133 2 ″ ″ 70 79 10 PIFNPEWQTP 127 A*3201 36 0,51 19 2 ″ ″ 71 81 11 IFNPEWQTPSF 128 A*2301 95 1,19 112 2 ″ ″ 71 81 11 IFNPEWQTPSF ″ A*2402 79 ″ 94 2 ″ ″ 73 81 9 NPEWQTPSF 129 B*0702 55 ″ 65 2 ″ ″ 73 81 9 NPEWQTPSF ″ B*3501 92 ″ 109 2 ″ ″ 73 81 9 NPEWQTPSF ″ B*3503 62 ″ 74 2 ″ ″ 73 81 9 NPEWQTPSF ″ B*5301 84 ″ 99 2 ″ ″ 74 81 8 PEWQTPSF 130 B*1801 71 ″ 85 2 ″ ″ 74 81 8 PEWQTPSF ″ B*4402 62 ″ 73 2 ″ ″ 74 81 8 PEWQTPSF ″ B*4403 72 ″ 85 2 ″ ″ 76 83 8 WQTPSFPK 131 A*1101 7 0,81 5 2 ″ ″ 74 84 11 PEWQTPSFPKI 132 B*1301 82 1,32 108 2 ″ ″ 74 84 11 PEWQTPSFPKI ″ B*1302 15 ″ 20 2 ″ ″ 74 84 11 PEWQTPSFPKI ″ B*4001 4 ″ 6 2 ″ ″ 74 84 11 PEWQTPSFPKI ″ B*4402 31 ″ 41 2 ″ ″ 74 84 11 PEWQTPSFPKI ″ B*4403 36 ″ 48 2 ″ ″ 74 84 11 PEWQTPSFPKI ″ B*4901 78 ″ 103 2 ″ ″ 76 84 9 WQTPSFPKI 133 A*0206 67 ″ 88 2 ″ ″ 76 84 9 WQTPSFPKI ″ B*1301 99 ″ 130 2 ″ ″ 76 84 9 WQTPSFPKI ″ B*1302 51 ″ 67 2 ″ ″ 76 84 9 WQTPSFPKI ″ B*3701 38 ″ 50 2 ″ ″ 76 84 9 WQTPSFPKI ″ B*4801 10 ″ 13 2 ″ ″ 76 84 9 WQTPSFPKI ″ B*4901 17 ″ 23 2 ″ ″ 76 84 9 WQTPSFPKI ″ B*5201 100 ″ 132 2 ″ ″ 76 86 11 WQTPSFPKIHL 134 B*1301 86 1,51 130 2 ″ ″ 76 86 11 WQTPSFPKIHL ″ B*1302 14 ″ 21 2 ″ ″ 76 86 11 WQTPSFPKIHL ″ B*3701 33 ″ 50 2 ″ ″ 76 86 11 WQTPSFPKIHL ″ B*3801 59 ″ 89 2 ″ ″ 76 86 11 WQTPSFPKIHL ″ B*3901 44 ″ 67 2 ″ ″ 76 86 11 WQTPSFPKIHL ″ B*4001 30 ″ 46 2 ″ ″ 76 86 11 WQTPSFPKIHL ″ B*4801 83 ″ 125 2 ″ ″ 78 86 9 TPSFPKIHL 135 B*0702 10 ″ 15 2 ″ ″ Cumulative BCI Class I score: 6943 104 111 8 NEKRRLKL 136 B*0801 83 1,27 105 3 103 135 104 112 9 NEKRRLKLI 137 B*4402 42 0,71 30 3 ″ ″ 104 112 9 NEKRRLKLI ″ B*4901 4 ″ 3 3 ″ ″ 106 113 8 KRRLKLIM 138 B*2702 69 0,90 62 3 ″ ″ 106 113 8 KRRLKLIM ″ B*2705 49 ″ 44 3 ″ ″ 107 114 8 RRLKLIMP 139 B*2702 39 0,23 9 3 ″ ″ 107 114 8 RRLKLIMP ″ B*2705 100 ″ 23 3 ″ ″ 106 115 10 KRRLKLIMPA 140 B*2705 16 1,60 26 3 ″ ″ 107 115 9 RRLKLIMPA 141 B*2702 93 ″ 148 3 ″ ″ 107 115 9 RRLKLIMPA ″ B*2705 99 ″ 157 3 ″ ″ 108 115 8 RLKLIMPA 142 A*3001 52 ″ 83 3 ″ ″ 108 115 8 RLKLIMPA ″ B*0801 46 ″ 73 3 ″ ″ 106 116 11 KRRLKLIMPAR 143 B*2705 42 0,86 36 3 ″ ″ 107 116 10 RRLKLIMPAR 144 A*3101 49 ″ 42 3 ″ ″ 107 116 10 RRLKLIMPAR ″ B*2702 63 ″ 54 3 ″ ″ 107 116 10 RRLKLIMPAR ″ B*2705 97 ″ 83 3 ″ ″ 108 116 9 RLKLIMPAR 145 A*3101 96 ″ 83 3 ″ ″ 108 116 9 RLKLIMPAR ″ A*3303 61 ″ 52 3 ″ ″ 108 116 9 RLKLIMPAR ″ A*7401 91 ″ 78 3 ″ ″ 107 117 11 RRLKLIMPARF 146 B*2705 78 1,18 91 3 ″ ″ 108 117 10 RLKLIMPARF 147 B*1501 16 ″ 18 3 ″ ″ 110 117 8 KLIMPARF 148 A*2301 9 ″ 10 3 ″ ″ 110 117 8 KLIMPARF ″ A*3201 95 ″ 112 3 ″ ″ 110 117 8 KLIMPARF ″ B*1501 55 ″ 64 3 ″ ″ 110 117 8 KLIMPARF ″ B*1525 58 ″ 68 3 ″ ″ 108 118 11 RLKLIMPARFY 149 A*0301 34 1,43 49 3 ″ ″ 108 118 11 RLKLIMPARFY ″ A*3001 32 ″ 45 3 ″ ″ 108 118 11 RLKLIMPARFY ″ A*3002 92 ″ 131 3 ″ ″ 108 118 11 RLKLIMPARFY ″ B*1501 14 ″ 20 3 ″ ″ 109 118 10 LKLIMPARFY 150 A*2902 35 ″ 50 3 ″ ″ 110 118 9 KLIMPARFY 151 A*0301 38 ″ 54 3 ″ ″ 110 118 9 KLIMPARFY ″ A*3002 75 ″ 107 3 ″ ″ 111 118 8 LIMPARFY 152 A*2902 71 ″ 102 3 ″ ″ 111 118 8 LIMPARFY ″ A*3002 68 ″ 97 3 ″ ″ 111 118 8 LIMPARFY ″ B*1501 45 ″ 65 3 ″ ″ 111 118 8 LIMPARFY ″ B*1502 50 ″ 71 3 ″ ″ 111 118 8 LIMPARFY ″ B*1525 27 ″ 39 3 ″ ″ 111 118 8 LIMPARFY ″ B*3501 24 ″ 34 3 ″ ″ 111 120 10 LIMPARFYPT 153 A*0206 77 0,18 13 3 ″ ″ 113 120 8 MPARFYPT 154 A*6802 21 ″ 4 3 ″ ″ 113 120 8 MPARFYPT ″ B*0801 58 ″ 10 3 ″ ″ 113 120 8 MPARFYPT ″ B*1402 35 ″ 6 3 ″ ″ 113 120 8 MPARFYPT ″ B*3503 80 ″ 14 3 ″ ″ 113 120 8 MPARFYPT ″ B*5101 75 ″ 13 3 ″ ″ 113 120 8 MPARFYPT ″ B*5301 23 ″ 4 3 ″ ″ 113 120 8 MPARFYPT ″ B*5501 100 ″ 18 3 ″ ″ 113 121 9 MPARFYPTH 155 B*3501 84 1,01 85 3 ″ ″ 113 121 9 MPARFYPTH ″ B*3503 23 ″ 23 3 ″ ″ 113 121 9 MPARFYPTH ″ B*5301 62 ″ 63 3 ″ ″ 113 121 9 MPARFYPTH ″ B*5501 57 ″ 58 3 ″ ″ 113 121 9 MPARFYPTH ″ B*5601 45 ″ 45 3 ″ ″ 113 122 10 MPARFYPTHT 156 B*3501 23 0,98 22 3 ″ ″ 113 122 10 MPARFYPTHT ″ B*3503 19 ″ 19 3 ″ ″ 113 122 10 MPARFYPTHT ″ B*5301 10 ″ 10 3 ″ ″ 113 122 10 MPARFYPTHT ″ B*5501 73 ″ 72 3 ″ ″ 113 122 10 MPARFYPTHT ″ B*5601 81 ″ 79 3 ″ ″ 115 122 8 ARFYPTHT 157 B*2705 15 ″ 15 3 ″ ″ 113 123 11 MPARFYPTHTK 158 B*5501 49 1,38 67 3 ″ ″ 113 123 11 MPARFYPTHTK ″ B*5601 54 ″ 74 3 ″ ″ 115 123 9 ARFYPTHTK 159 B*2705 87 ″ 119 3 ″ ″ 116 123 8 RFYPTHTK 160 A*0301 84 ″ 115 3 ″ ″ 116 123 8 RFYPTHTK ″ A*3001 79 ″ 109 3 ″ ″ 116 123 8 RFYPTHTK ″ A*3101 76 ″ 105 3 ″ ″ 116 123 8 RFYPTHTK ″ A*7401 57 ″ 79 3 ″ ″ 115 124 10 ARFYPTHTKY 161 A*2902 6 1,50 10 3 ″ ″ 115 124 10 ARFYPTHTKY ″ B*2702 61 ″ 92 3 ″ ″ 115 124 10 ARFYPTHTKY ″ B*2705 55 ″ 83 3 ″ ″ 116 124 9 RFYPTHTKY 162 A*2902 92 ″ 138 3 ″ ″ 116 124 9 RFYPTHTKY ″ A*3002 1 ″ 2 3 ″ ″ 117 124 8 FYPTHTKY 163 B*3501 51 ″ 76 3 ″ ″ 115 125 11 ARFYPTHTKYL 164 B*2702 67 1,93 130 3 ″ ″ 115 125 11 ARFYPTHTKYL ″ B*2705 34 ″ 66 3 ″ ″ 116 125 10 RFYPTHTKYL 165 B*4801 4 ″ 7 3 ″ ″ 117 125 9 FYPTHTKYL 166 A*2402 39 ″ 74 3 ″ ″ 118 125 8 YPTHTKYL 167 B*1402 42 ″ 82 3 ″ ″ 118 125 8 YPTHTKYL ″ B*3501 17 ″ 33 3 ″ ″ 118 125 8 YPTHTKYL ″ B*3503 78 ″ 151 3 ″ ″ 118 125 8 YPTHTKYL ″ B*5101 43 ″ 83 3 ″ ″ 118 125 8 YPTHTKYL ″ B*5301 51 ″ 98 3 ″ ″ 118 125 8 YPTHTKYL ″ B*5501 31 ″ 60 3 ″ ″ 117 126 10 FYPTHTKYLP 168 A*2402 54 0,14 7 3 ″ ″ 118 126 9 YPTHTKYLP 169 B*5301 2 ″ 0 3 ″ ″ 117 127 11 FYPTHTKYLPL 170 A*2301 52 0,94 49 3 ″ ″ 117 127 11 FYPTHTKYLPL ″ A*2402 56 ″ 53 3 ″ ″ 118 127 10 YPTHTKYLPL 171 B*0702 65 ″ 61 3 ″ ″ 118 127 10 YPTHTKYLPL ″ B*1402 100 ″ 94 3 ″ ″ 118 127 10 YPTHTKYLPL ″ B*3501 75 ″ 70 3 ″ ″ 118 127 10 YPTHTKYLPL ″ B*3503 100 ″ 94 3 ″ ″ 118 127 10 YPTHTKYLPL ″ B*3901 96 ″ 90 3 ″ ″ 118 127 10 YPTHTKYLPL ″ B*5101 83 ″ 78 3 ″ ″ 118 127 10 YPTHTKYLPL ″ B*5301 82 ″ 77 3 ″ ″ 118 127 10 YPTHTKYLPL ″ B*5501 87 ″ 82 3 ″ ″ 118 127 10 YPTHTKYLPL ″ B*5601 67 ″ 63 3 ″ ″ 120 127 8 THTKYLPL 172 B*1402 95 ″ 89 3 ″ ″ 120 127 8 THTKYLPL ″ B*3801 80 ″ 75 3 ″ ″ 119 128 10 PTHTKYLPLD 173 A*3001 46 0,71 33 3 ″ ″ 121 129 9 HTKYLPLDK 174 A*0301 18 0,41 7 3 ″ ″ 121 129 9 HTKYLPLDK ″ A*3001 90 ″ 37 3 ″ ″ 123 131 9 KYLPLDKGI 175 A*2301 34 1,23 43 3 ″ ″ 123 131 9 KYLPLDKGI ″ A*2402 21 ″ 26 3 ″ ″ 125 132 8 LPLDKGIK 176 B*3501 56 0,80 45 3 ″ ″ 125 134 10 LPLDKGIKPY 177 B*3501 87 1,08 94 3 ″ ″ 125 134 10 LPLDKGIKPY ″ B*3503 36 ″ 39 3 ″ ″ 125 134 10 LPLDKGIKPY ″ B*5301 39 ″ 43 3 ″ ″ 125 134 10 LPLDKGIKPY ″ B*5501 13 ″ 14 3 ″ ″ 126 134 9 PLDKGIKPY 178 A*0101 25 ″ 27 3 ″ ″ 127 134 8 LDKGIKPY 179 B*3501 9 ″ 10 3 ″ ″ 125 135 11 LPLDKGIKPYY 180 B*3501 77 1,16 90 3 ″ ″ 125 135 11 LPLDKGIKPYY ″ B*5301 57 ″ 67 3 ″ ″ 126 135 10 PLDKGIKPYY 181 A*0101 55 ″ 64 3 ″ ″ 126 135 10 PLDKGIKPYY ″ A*2902 3 ″ 4 3 ″ ″ Cumulative Class I-BCI score: 6469 118 127 10 YPTHTKYLPL 171 B*0702 65 0,94 61 4 118 150 118 127 10 YPTHTKYLPL ″ B*1402 100 ″ 94 4 ″ ″ 118 127 10 YPTHTKYLPL ″ B*3501 75 ″ 70 4 ″ ″ 118 127 10 YPTHTKYLPL ″ B*3503 100 ″ 94 4 ″ ″ 118 127 10 YPTHTKYLPL ″ B*3901 96 ″ 90 4 ″ ″ 118 127 10 YPTHTKYLPL ″ B*5101 83 ″ 78 4 ″ ″ 118 127 10 YPTHTKYLPL ″ B*5301 82 ″ 77 4 ″ ″ 118 127 10 YPTHTKYLPL ″ B*5501 87 ″ 82 4 ″ ″ 118 127 10 YPTHTKYLPL ″ B*5601 67 ″ 63 4 ″ ″ 120 127 8 THTKYLPL 172 B*1402 95 ″ 89 4 ″ ″ 120 127 8 THTKYLPL ″ B*3801 80 ″ 75 4 ″ ″ 119 128 10 PTHTKYLPLD 173 A*3001 46 0,71 33 4 ″ ″ 121 129 9 HTKYLPLDK 174 A*0301 18 0,41 7 4 ″ ″ 121 129 9 HTKYLPLDK ″ A*3001 90 ″ 37 4 ″ ″ 123 131 9 KYLPLDKGI 175 A*2301 34 1,23 43 4 ″ ″ 123 131 9 KYLPLDKGI ″ A*2402 21 ″ 26 4 ″ ″ 125 132 8 LPLDKGIK 176 B*3501 56 0,80 45 4 ″ ″ 125 134 10 LPLDKGIKPY 177 B*3501 87 1,08 94 4 ″ ″ 125 134 10 LPLDKGIKPY ″ B*3503 36 ″ 39 4 ″ ″ 125 134 10 LPLDKGIKPY ″ B*5301 39 ″ 43 4 ″ ″ 125 134 10 LPLDKGIKPY ″ B*5501 13 ″ 14 4 ″ ″ 126 134 9 PLDKGIKPY 178 A*0101 25 ″ 27 4 ″ ″ 127 134 8 LDKGIKPY 179 B*3501 9 ″ 10 4 ″ ″ 125 135 11 LPLDKGIKPYY 180 B*3501 77 1,16 90 4 ″ ″ 125 135 11 LPLDKGIKPYY ″ B*5301 57 ″ 67 4 ″ ″ 126 135 10 PLDKGIKPYY 181 A*0101 55 ″ 64 4 ″ ″ 126 135 10 PLDKGIKPYY ″ A*2902 3 ″ 4 4 ″ ″ 132 139 8 KPYYPDQV 182 B*5101 65 1,05 68 4 ″ ″ 132 139 8 KPYYPDQV ″ B*5501 64 ″ 67 4 ″ ″ 132 139 8 KPYYPDQV ″ B*5601 59 ″ 62 4 ″ ″ 132 140 9 KPYYPDQVV 183 B*0702 36 1,80 65 4 ″ ″ 132 140 9 KPYYPDQVV ″ B*5101 70 ″ 126 4 ″ ″ 132 140 9 KPYYPDQVV ″ B*5501 86 ″ 155 4 ″ ″ 132 140 9 KPYYPDQVV ″ B*5601 65 ″ 118 4 ″ ″ 135 142 8 YPDQVVNH 184 B*3501 89 1,63 146 4 ″ ″ 134 143 10 YYPDQVVNHY 185 A*0101 23 1,33 30 4 ″ ″ 134 143 10 YYPDQVVNHY ″ A*2402 25 ″ 33 4 ″ ″ 134 143 10 YYPDQVVNHY ″ A*2902 65 ″ 87 4 ″ ″ 134 143 10 YYPDQVVNHY ″ A*3002 25 ″ 34 4 ″ ″ 135 143 9 YPDQVVNHY 186 A*0101 62 ″ 83 4 ″ ″ 135 143 9 YPDQVVNHY ″ B*3501 83 ″ 110 4 ″ ″ 135 143 9 YPDQVVNHY ″ B*3503 55 ″ 74 4 ″ ″ 135 143 9 YPDQVVNHY ″ B*5301 44 ″ 59 4 ″ ″ 136 143 8 PDQVVNHY 187 B*3501 4 ″ 5 4 ″ ″ 134 144 11 YYPDQVVNHYF 188 A*2301 100 1,77 177 4 ″ ″ 135 144 10 YPDQVVNHYF 189 B*3501 100 ″ 177 4 ″ ″ 135 144 10 YPDQVVNHYF ″ B*3503 95 ″ 168 4 ″ ″ 135 144 10 YPDQVVNHYF ″ B*5301 100 ″ 177 4 ″ ″ 137 144 8 DQVVNHYF 190 B*1801 52 ″ 93 4 ″ ″ 137 147 11 DQVVNHYFQTR 191 A*3303 21 1,63 34 4 ″ ″ 138 147 10 QVVNHYFQTR 192 A*3101 1 ″ 2 4 ″ ″ 138 147 10 QVVNHYFQTR ″ A*3303 86 ″ 140 4 ″ ″ 138 147 10 QVVNHYFQTR ″ A*6801 68 ″ 110 4 ″ ″ 138 147 10 QVVNHYFQTR ″ A*7401 17 ″ 28 4 ″ ″ 139 147 9 VVNHYFQTR 193 A*3101 87 ″ 143 4 ″ ″ 139 147 9 VVNHYFQTR ″ A*3303 73 ″ 120 4 ″ ″ 139 147 9 VVNHYFQTR ″ A*7401 72 ″ 117 4 ″ ″ 139 149 11 VVNHYFQTRHY 194 A*0101 42 1,90 79 4 ″ ″ 139 149 11 VVNHYFQTRHY ″ A*2902 70 ″ 133 4 ″ ″ 139 149 11 VVNHYFQTRHY ″ A*3002 90 ″ 172 4 ″ ″ 139 149 11 VVNHYFQTRHY ″ B*1501 50 ″ 95 4 ″ ″ 139 149 11 VVNHYFQTRHY ″ B*1502 44 ″ 85 4 ″ ″ 141 149 9 NHYFQTRHY 195 B*3801 16 ″ 31 4 ″ ″ 142 149 8 HYFQTRHY 196 A*2902 25 ″ 48 4 ″ ″ 142 149 8 HYFQTRHY ″ A*3002 44 ″ 83 4 ″ ″ 141 150 10 NHYFQTRHYL 197 B*1402 94 1,93 181 4 ″ ″ 141 150 10 NHYFQTRHYL ″ B*3801 53 ″ 102 4 ″ ″ 141 150 10 NHYFQTRHYL ″ B*3901 88 ″ 170 4 ″ ″ 142 150 9 HYFQTRHYL 198 A*2301 69 ″ 133 4 ″ ″ 142 150 9 HYFQTRHYL ″ B*1402 34 ″ 66 4 ″ ″ 142 150 9 HYFQTRHYL ″ B*3901 3 ″ 5 4 ″ ″ 143 150 8 YFQTRHYL 199 A*2301 74 ″ 143 4 ″ ″ 143 150 8 YFQTRHYL ″ A*2402 74 ″ 142 4 ″ ″ 143 150 8 YFQTRHYL ″ B*0801 93 ″ 180 4 ″ ″ Cumulative Class I-BCI score: 6169 139 149 11 VVNHYFQTRHY 194 A*0101 42 1,90 79 5 139 177 139 149 11 VVNHYFQTRHY ″ A*2902 70 ″ 133 5 ″ ″ 139 149 11 VVNHYFQTRHY ″ A*3002 90 ″ 172 5 ″ ″ 139 149 11 VVNHYFQTRHY ″ B*1501 50 ″ 95 5 ″ ″ 139 149 11 VVNHYFQTRHY ″ B*1502 44 ″ 85 5 ″ ″ 141 149 9 NHYFQTRHY 195 B*3801 16 ″ 31 5 ″ ″ 142 149 8 HYFQTRHY 196 A*2902 25 ″ 48 5 ″ ″ 142 149 8 HYFQTRHY ″ A*3002 44 ″ 83 5 ″ ″ 141 150 10 NHYFQTRHYL 197 B*1402 94 1,93 181 5 ″ ″ 141 150 10 NHYFQTRHYL ″ B*3801 53 ″ 102 5 ″ ″ 141 150 10 NHYFQTRHYL ″ B*3901 88 ″ 170 5 ″ ″ 142 150 9 HYFQTRHYL 198 A*2301 69 ″ 133 5 ″ ″ 142 150 9 HYFQTRHYL ″ B*1402 34 ″ 66 5 ″ ″ 142 150 9 HYFQTRHYL ″ B*3901 3 ″ 5 5 ″ ″ 143 150 8 YFQTRHYL 199 A*2301 74 ″ 143 5 ″ ″ 143 150 8 YFQTRHYL ″ A*2402 74 ″ 142 5 ″ ″ 143 150 8 YFQTRHYL ″ B*0801 93 ″ 180 5 ″ ″ 142 151 10 HYFQTRHYLH 200 A*2301 33 0,39 13 5 ″ ″ 142 151 10 HYFQTRHYLH ″ A*2402 49 ″ 19 5 ″ ″ 142 151 10 HYFQTRHYLH ″ A*2902 16 ″ 6 5 ″ ″ 143 151 9 YFQTRHYLH 201 A*2902 57 ″ 22 5 ″ ″ 143 153 11 YFQTRHYLHTL 202 A*2301 98 1,22 120 5 ″ ″ 143 153 11 YFQTRHYLHTL ″ A*2402 100 ″ 122 5 ″ ″ 143 153 11 YFQTRHYLHTL ″ B*0801 100 ″ 122 5 ″ ″ 144 153 10 FQTRhYLHTL 203 A*0201 27 ″ 33 5 ″ ″ 144 153 10 FQTRHYLHTL ″ B*1301 63 ″ 77 5 ″ ″ 144 153 10 FQTRHYLHTL ″ B*1402 52 ″ 63 5 ″ ″ 144 153 10 FQTRHYLHTL ″ B*3701 62 ″ 75 5 ″ ″ 144 153 10 FQTRHYLHTL ″ B*3801 71 ″ 87 5 ″ ″ 144 153 10 FQTRHYLHTL ″ B*3901 94 ″ 114 5 ″ ″ 144 153 10 FQTRHYLHTL ″ B*4801 81 ″ 98 5 ″ ″ 145 153 9 QTRHYLHTL 204 A*2501 65 ″ 79 5 ″ ″ 146 153 8 TRHYLHTL 205 B*1402 72 ″ 87 5 ″ ″ 146 153 8 TRHYLHTL ″ B*2702 60 ″ 73 5 ″ ″ 146 153 8 TRHYLHTL ″ B*2705 70 ″ 85 5 ″ ″ 144 154 11 FQTRHYLHTLW 206 B*1301 68 1,50 101 5 ″ ″ 144 154 11 FQTRHYLHTLW ″ B*2702 37 ″ 56 5 ″ ″ 145 154 10 QTRHYLHTLW 207 B*4402 35 ″ 52 5 ″ ″ 145 154 10 QTRHYLHTLW ″ B*5802 70 ″ 104 5 ″ ″ 146 154 9 TRHYLHTLW 208 B*2702 76 ″ 114 5 ″ ″ 147 154 8 RHYLHTLW 209 A*2301 47 ″ 70 5 ″ ″ 147 154 8 RHYLHTLW ″ A*2402 35 ″ 52 5 ″ ″ 147 154 8 RHYLHTLW ″ B*2702 99 ″ 148 5 ″ ″ 147 154 8 RHYLHTLW ″ B*3801 98 ″ 147 5 ″ ″ 147 154 8 RHYLHTLW ″ B*5701 35 ″ 52 5 ″ ″ 147 154 8 RHYLHTLW ″ B*5801 22 ″ 33 5 ″ ″ 147 154 8 RHYLHTLW ″ B*5802 26 ″ 39 5 ″ ″ 145 155 11 QTRHYLHTLWK 210 A*0301 54 0,72 39 5 ″ ″ 145 155 11 QTRHYLHTLWK ″ A*1101 35 ″ 25 5 ″ ″ 145 155 11 QTRHYLHTLWK ″ A*3001 96 ″ 69 5 ″ ″ 146 155 10 TRHYLHTLWK 211 B*2705 36 ″ 26 5 ″ ″ 147 155 9 RHYLHTLWK 212 A*0301 70 ″ 51 5 ″ ″ 147 155 9 RHYLHTLWK ″ B*2702 7 ″ 5 5 ″ ″ 148 155 8 HYLHTLWK 213 A*3101 29 ″ 21 5 ″ ″ 146 156 11 TRHYLHTLWKA 214 B*2705 58 1,23 72 5 ″ ″ 148 156 9 HYLHTLWKA 215 A*2301 31 ″ 38 5 ″ ″ 147 157 11 RHYLHTLWKAG 216 B*2705 6 0,73 4 5 ″ ″ 148 157 10 HYLHTLWKAG 217 A*3201 74 ″ 54 5 ″ ″ 148 158 11 HYLHTLWKAGI 218 A*2301 93 0,63 59 5 ″ ″ 148 158 11 HYLHTLWKAGI ″ A*2402 95 ″ 60 5 ″ ″ 149 158 10 YLHTLWKAGI 219 A*0201 7 ″ 4 5 ″ ″ 151 158 8 HTLWKAGI 220 A*3201 62 ″ 39 5 ″ ″ 149 159 11 YLHTLWKAGIL 221 B*0801 88 0,85 75 5 ″ ″ 149 159 11 YLHTLWKAGIL ″ B*3901 22 ″ 19 5 ″ ″ 150 159 10 LHTLWKAGIL 222 B*0801 69 ″ 59 5 ″ ″ 150 159 10 LHTLWKAGIL ″ B*3801 51 ″ 43 5 ″ ″ 150 159 10 LHTLWKAGIL ″ B*3901 34 ″ 29 5 ″ ″ 151 159 9 HTLWKAGIL 223 B*5802 1 ″ 1 5 ″ ″ 151 160 10 HTLWKAGILY 224 A*0101 72 1,87 134 5 ″ ″ 151 160 10 HTLWKAGILY ″ A*0301 7 ″ 12 5 ″ ″ 151 160 10 HTLWKAGILY ″ A*2501 47 ″ 88 5 ″ ″ 151 160 10 HTLWKAGILY ″ A*2601 67 ″ 125 5 ″ ″ 151 160 10 HTLWKAGILY ″ A*2902 2 ″ 3 5 ″ ″ 151 160 10 HTLWKAGILY ″ A*3002 49 ″ 92 5 ″ ″ 152 160 9 TLWKAGILY 225 A*0301 36 ″ 67 5 ″ ″ 152 160 9 TLWKAGILY ″ A*2902 78 ″ 145 5 ″ ″ 152 160 9 TLWKAGILY ″ A*3002 4 ″ 8 5 ″ ″ 153 160 8 LWKAGILY 226 A*2902 56 ″ 104 5 ″ ″ 153 160 8 LWKAGILY ″ A*3002 85 ″ 158 5 ″ ″ 153 160 8 LWKAGILY ″ B*3501 8 ″ 15 5 ″ ″ 151 161 11 HTLWKAGILYK 227 A*0301 89 1,41 125 5 ″ ″ 151 161 11 HTLWKAGILYK ″ A*1101 100 ″ 141 5 ″ ″ 151 161 11 HTLWKAGILYK ″ A*3001 78 ″ 110 5 ″ ″ 151 161 11 HTLWKAGILYK ″ A*3101 46 ″ 64 5 ″ ″ 151 161 11 HTLWKAGILYK ″ A*3303 25 ″ 36 5 ″ ″ 151 161 11 HTLWKAGILYK ″ A*6801 75 ″ 106 5 ″ ″ 151 161 11 HTLWKAGILYK ″ A*7401 83 ″ 117 5 ″ ″ 152 161 10 TLWKAGILYK 228 A*0301 87 ″ 122 5 ″ ″ 152 161 10 TLWKAGILYK ″ A*1101 59 ″ 83 5 ″ ″ 152 161 10 TLWKAGILYK ″ A*7401 71 ″ 100 5 ″ ″ 153 161 9 LWKAGILYK 229 A*3001 57 ″ 80 5 ″ ″ 152 162 11 TLWKAGILYKR 230 A*3101 61 1,49 91 5 ″ ″ 152 162 11 TLWKAGILYKR ″ A*3303 72 ″ 107 5 ″ ″ 152 162 11 TLWKAGILYKR ″ A*7401 82 ″ 122 5 ″ ″ 153 162 10 LWKAGILYKR 231 A*3101 86 ″ 128 5 ″ ″ 153 162 10 LWKAGILYKR ″ A*3303 59 ″ 88 5 ″ ″ 155 162 8 KAGILYKR 232 A*3101 67 ″ 100 5 ″ ″ 155 162 8 KAGILYKR ″ A*7401 27 ″ 40 5 ″ ″ 158 166 9 ILYKRETTR 233 A*0301 66 1,75 115 5 ″ ″ 158 166 9 ILYKRETTR ″ A*3101 23 ″ 40 5 ″ ″ 158 166 9 ILYKRETTR ″ A*3303 51 ″ 89 5 ″ ″ 158 166 9 ILYKRETTR ″ A*7401 90 ″ 158 5 ″ ″ 158 168 11 ILYKRETTRSA 234 B*0801 56 1,80 100 5 ″ ″ 160 170 11 YKRETTRSASF 235 B*0702 17 1,82 32 5 ″ ″ 160 170 11 YKRETTRSASF ″ B*0801 81 ″ 148 5 ″ ″ 160 170 11 YKRETTRSASF ″ B*1402 68 ″ 123 5 ″ ″ 160 170 11 YKRETTRSASF ″ B*1501 53 ″ 97 5 ″ ″ 160 170 11 YKRETTRSASF ″ B*1502 65 ″ 118 5 ″ ″ 160 170 11 YKRETTRSASF ″ B*1525 46 ″ 83 5 ″ ″ 161 170 10 KRETTRSASF 236 B*2702 53 ″ 97 5 ″ ″ 162 170 9 RETTRSASF 237 B*4001 57 ″ 103 5 ″ ″ 162 170 9 RETTRSASF ″ B*4402 88 ″ 161 5 ″ ″ 162 170 9 RETTRSASF ″ B*4403 60 ″ 109 5 ″ ″ 162 170 9 RETTRSASF ″ B*5001 44 ″ 80 5 ″ ″ 163 170 8 ETTRSASF 238 A*2501 100 ″ 182 5 ″ ″ 163 170 8 ETTRSASF ″ A*2601 100 ″ 182 5 ″ ″ 166 175 10 RSASFCGSPY 239 A*0101 79 1,16 92 5 ″ ″ 166 175 10 RSASFCGSPY ″ A*2501 45 ″ 52 5 ″ ″ 166 175 10 RSASFCGSPY ″ B*1501 94 ″ 108 5 ″ ″ 166 175 10 RSASFCGSPY ″ B*1502 78 ″ 90 5 ″ ″ 166 175 10 RSASFCGSPY ″ B*1525 80 ″ 92 5 ″ ″ 166 175 10 RSASFCGSPY ″ B*4403 32 ″ 37 5 ″ ″ 166 175 10 RSASFCGSPY ″ B*4601 84 ″ 97 5 ″ ″ 166 175 10 RSASFCGSPY ″ B*5802 68 ″ 79 5 ″ ″ 167 175 9 SASFCGSPY 240 A*3002 79 ″ 91 5 ″ ″ 167 175 9 SASFCGSPY ″ B*3501 81 ″ 94 5 ″ ″ 168 175 8 ASFCGSPY 241 A*1101 70 ″ 80 5 ″ ″ 168 175 8 ASFCGSPY ″ A*2902 54 ″ 62 5 ″ ″ 168 175 8 ASFCGSPY ″ B*5701 44 ″ 51 5 ″ ″ 167 176 10 SASFCGSPYS 242 A*3001 8 0,16 1 5 ″ ″ 167 176 10 SASFCGSPYS ″ B*5701 76 ″ 12 5 ″ ″ 167 176 10 SASFCGSPYS ″ B*5801 76 ″ 12 5 ″ ″ 168 176 9 ASFCGSPYS 243 B*5802 19 ″ 3 5 ″ ″ 167 177 11 SASFCGSPYSW 244 B*5301 79 1,90 150 5 ″ ″ 167 177 11 SASFCGSPYSW ″ B*5701 94 ″ 179 5 ″ ″ 167 177 11 SASFCGSPYSW ″ B*5801 100 ″ 190 5 ″ ″ 167 177 11 SASFCGSPYSW ″ B*5802 100 ″ 190 5 ″ ″ 168 177 10 ASFCGSPYSW 245 B*4402 69 ″ 132 5 ″ ″ 168 177 10 ASFCGSPYSW ″ B*4403 28 ″ 53 5 ″ ″ 168 177 10 ASFCGSPYSW ″ B*5802 99 ″ 188 5 ″ ″ 169 177 9 SFCGSPYSW 246 A*2301 26 ″ 49 5 ″ ″ Cumulative BCI Class Iscore: 11815 143 150 8 YFQTRHYL 199 A*2301 74 1,93 143 6 143 177 143 150 8 YFQTRHYL ″ A*2402 74 ″ 142 6 ″ ″ 143 150 8 YFQTRHYL ″ B*0801 93 ″ 180 6 ″ ″ 142 151 10 HYFQTRHYLH 200 A*2301 33 0,39 13 6 ″ ″ 142 151 10 HYFQTRHYLH ″ A*2402 49 ″ 19 6 ″ ″ 142 151 10 HYFQTRHYLH ″ A*2902 16 ″ 6 6 ″ ″ 143 151 9 YFQTRHYLH 201 A*2902 57 ″ 22 6 ″ ″ 143 153 11 YFQTRHYLHTL 202 A*2301 98 1,22 120 6 ″ ″ 143 153 11 YFQTRHYLHTL ″ A*2402 100 ″ 122 6 ″ ″ 143 153 11 YFQTRHYLHTL ″ B*0801 100 ″ 122 6 ″ ″ 144 153 10 FQTRhYLHTL 203 A*0201 27 ″ 33 6 ″ ″ 144 153 10 FQTRHYLHTL ″ B*1301 63 ″ 77 6 ″ ″ 144 153 10 FQTRHYLHTL ″ B*1402 52 ″ 63 6 ″ ″ 144 153 10 FQTRHYLHTL ″ B*3701 62 ″ 75 6 ″ ″ 144 153 10 FQTRHYLHTL ″ B*3801 71 ″ 87 6 ″ ″ 144 153 10 FQTRHYLHTL ″ B*3901 94 ″ 114 6 ″ ″ 144 153 10 FQTRHYLHTL ″ B*4801 81 ″ 98 6 ″ ″ 145 153 9 QTRHYLHTL 204 A*2501 65 ″ 79 6 ″ ″ 146 153 8 TRHYLHTL 205 B*1402 72 ″ 87 6 ″ ″ 146 153 8 TRHYLHTL ″ B*2702 60 ″ 73 6 ″ ″ 146 153 8 TRHYLHTL ″ B*2705 70 ″ 85 6 ″ ″ 144 154 11 FQTRHYLHTLW 206 B*1301 68 1,50 101 6 ″ ″ 144 154 11 FQTRHYLHTLW ″ B*2702 37 ″ 56 6 ″ ″ 145 154 10 QTRHYLHTLW 207 B*4402 35 ″ 52 6 ″ ″ 145 154 10 QTRHYLHTLW ″ B*5802 70 ″ 104 6 ″ ″ 146 154 9 TRHYLHTLW 208 B*2702 76 ″ 114 6 ″ ″ 147 154 8 RHYLHTLW 209 A*2301 47 ″ 70 6 ″ ″ 147 154 8 RHYLHTLW ″ A*2402 35 ″ 52 6 ″ ″ 147 154 8 RHYLHTLW ″ B*2702 99 ″ 148 6 ″ ″ 147 154 8 RHYLHTLW ″ B*3801 98 ″ 147 6 ″ ″ 147 154 8 RHYLHTLW ″ B*5701 35 ″ 52 6 ″ ″ 147 154 8 RHYLHTLW ″ B*5801 22 ″ 33 6 ″ ″ 147 154 8 RHYLHTLW ″ B*5802 26 ″ 39 6 ″ ″ 145 155 11 QTRHYLHTLWK 210 A*0301 54 0,72 39 6 ″ ″ 145 155 11 QTRHYLHTLWK ″ A*1101 35 ″ 25 6 ″ ″ 145 155 11 QTRHYLHTLWK ″ A*3001 96 ″ 69 6 ″ ″ 146 155 10 TRHYLHTLWK 211 B*2705 36 ″ 26 6 ″ ″ 147 155 9 RHYLHTLWK 212 A*0301 70 ″ 51 6 ″ ″ 147 155 9 RHYLHTLWK ″ B*2702 7 ″ 5 6 ″ ″ 148 155 8 HYLHTLWK 213 A*3101 29 ″ 21 6 ″ ″ 146 156 11 TRHYLHTLWKA 214 B*2705 58 1,23 72 6 ″ ″ 148 156 9 HYLHTLWKA 215 A*2301 31 ″ 38 6 ″ ″ 147 157 11 RHYLHTLWKAG 216 B*2705 6 0,73 4 6 ″ ″ 148 157 10 HYLHTLWKAG 217 A*3201 74 ″ 54 6 ″ ″ 148 158 11 HYLHTLWKAGI 218 A*2301 93 0,63 59 6 ″ ″ 148 158 11 HYLHTLWKAGI ″ A*2402 95 ″ 60 6 ″ ″ 149 158 10 YLHTLWKAGI 219 A*0201 7 ″ 4 6 ″ ″ 151 158 8 HTLWKAGI 220 A*3201 62 ″ 39 6 ″ ″ 149 159 11 YLHTLWKAGIL 221 B*0801 88 0,85 75 6 ″ ″ 149 159 11 YLHTLWKAGIL ″ B*3901 22 ″ 19 6 ″ ″ 150 159 10 LHTLWKAGIL 222 B*0801 69 ″ 59 6 ″ ″ 150 159 10 LHTLWKAGIL ″ B*3801 51 ″ 43 6 ″ ″ 150 159 10 LHTLWKAGIL ″ B*3901 34 ″ 29 6 ″ ″ 151 159 9 HTLWKAGIL 223 B*5802 1 ″ 1 6 ″ ″ 151 160 10 HTLWKAGILY 224 A*0101 72 1,87 134 6 ″ ″ 151 160 10 HTLWKAGILY ″ A*0301 7 ″ 12 6 ″ ″ 151 160 10 HTLWKAGILY ″ A*2501 47 ″ 88 6 ″ ″ 151 160 10 HTLWKAGILY ″ A*2601 67 ″ 125 6 ″ ″ 151 160 10 HTLWKAGILY ″ A*2902 2 ″ 3 6 ″ ″ 151 160 10 HTLWKAGILY ″ A*3002 49 ″ 92 6 ″ ″ 152 160 9 TLWKAGILY 225 A*0301 36 ″ 67 6 ″ ″ 152 160 9 TLWKAGILY ″ A*2902 78 ″ 145 6 ″ ″ 152 160 9 TLWKAGILY ″ A*3002 4 ″ 8 6 ″ ″ 153 160 8 LWKAGILY 226 A*2902 56 ″ 104 6 ″ ″ 153 160 8 LWKAGILY ″ A*3002 85 ″ 158 6 ″ ″ 153 160 8 LWKAGILY ″ B*3501 8 ″ 15 6 ″ ″ 151 161 11 HTLWKAGILYK 227 A*0301 89 1,41 125 6 ″ ″ 151 161 11 HTLWKAGILYK ″ A*1101 100 ″ 141 6 ″ ″ 151 161 11 HTLWKAGILYK ″ A*3001 78 ″ 110 6 ″ ″ 151 161 11 HTLWKAGILYK ″ A*3101 46 ″ 64 6 ″ ″ 151 161 11 HTLWKAGILYK ″ A*3303 25 ″ 36 6 ″ ″ 151 161 11 HTLWKAGILYK ″ A*6801 75 ″ 106 6 ″ ″ 151 161 11 HTLWKAGILYK ″ A*7401 83 ″ 117 6 ″ ″ 152 161 10 TLWKAGILYK 228 A*0301 87 ″ 122 6 ″ ″ 152 161 10 TLWKAGILYK ″ A*1101 59 ″ 83 6 ″ ″ 152 161 10 TLWKAGILYK ″ A*7401 71 ″ 100 6 ″ ″ 153 161 9 LWKAGILYK 229 A*3001 57 ″ 80 6 ″ ″ 152 162 11 TLWKAGILYKR 230 A*3101 61 1,49 91 6 ″ ″ 152 162 11 TLWKAGILYKR ″ A*3303 72 ″ 107 6 ″ ″ 152 162 11 TLWKAGILYKR ″ A*7401 82 ″ 122 6 ″ ″ 153 162 10 LWKAGILYKR 231 A*3101 86 ″ 128 6 ″ ″ 153 162 10 LWKAGILYKR ″ A*3303 59 ″ 88 6 ″ ″ 155 162 8 KAGILYKR 232 A*3101 67 ″ 100 6 ″ ″ 155 162 8 KAGILYKR ″ A*7401 27 ″ 40 6 ″ ″ 158 166 9 ILYKRETTR 233 A*0301 66 1,75 115 6 ″ ″ 158 166 9 ILYKRETTR ″ A*3101 23 ″ 40 6 ″ ″ 158 166 9 ILYKRETTR ″ A*3303 51 ″ 89 6 ″ ″ 158 166 9 ILYKRETTR ″ A*7401 90 ″ 158 6 ″ ″ 158 168 11 ILYKRETTRSA 234 B*0801 56 1,80 100 6 ″ ″ 160 170 11 YKRETTRSASF 235 B*0702 17 1,82 32 6 ″ ″ 160 170 11 YKRETTRSASF ″ B*0801 81 ″ 148 6 ″ ″ 160 170 11 YKRETTRSASF ″ B*1402 68 ″ 123 6 ″ ″ 160 170 11 YKRETTRSASF ″ B*1501 53 ″ 97 6 ″ ″ 160 170 11 YKRETTRSASF ″ B*1502 65 ″ 118 6 ″ ″ 160 170 11 YKRETTRSASF ″ B*1525 46 ″ 83 6 ″ ″ 161 170 10 KRETTRSASF 236 B*2702 53 ″ 97 6 ″ ″ 162 170 9 RETTRSASF 237 B*4001 57 ″ 103 6 ″ ″ 162 170 9 RETTRSASF ″ B*4402 88 ″ 161 6 ″ ″ 162 170 9 RETTRSASF ″ B*4403 60 ″ 109 6 ″ ″ 162 170 9 RETTRSASF ″ B*5001 44 ″ 80 6 ″ ″ 163 170 8 ETTRSASF 238 A*2501 100 ″ 182 6 ″ ″ 163 170 8 ETTRSASF ″ A*2601 100 ″ 182 6 ″ ″ 166 175 10 RSASFCGSPY 239 A*0101 79 1,16 92 6 ″ ″ 166 175 10 RSASFCGSPY ″ A*2501 45 ″ 52 6 ″ ″ 166 175 10 RSASFCGSPY ″ B*1501 94 ″ 108 6 ″ ″ 166 175 10 RSASFCGSPY ″ B*1502 78 ″ 90 6 ″ ″ 166 175 10 RSASFCGSPY ″ B*1525 80 ″ 92 6 ″ ″ 166 175 10 RSASFCGSPY ″ B*4403 32 ″ 37 6 ″ ″ 166 175 10 RSASFCGSPY ″ B*4601 84 ″ 97 6 ″ ″ 166 175 10 RSASFCGSPY ″ B*5802 68 ″ 79 6 ″ ″ 167 175 9 SASFCGSPY 240 A*3002 79 ″ 91 6 ″ ″ 167 175 9 SASFCGSPY ″ B*3501 81 ″ 94 6 ″ ″ 168 175 8 ASFCGSPY 241 A*1101 70 ″ 80 6 ″ ″ 168 175 8 ASFCGSPY ″ A*2902 54 ″ 62 6 ″ ″ 168 175 8 ASFCGSPY ″ B*5701 44 ″ 51 6 ″ ″ 167 176 10 SASFCGSPYS 242 A*3001 8 0,16 1 6 ″ ″ 167 176 10 SASFCGSPYS ″ B*5701 76 ″ 12 6 ″ ″ 167 176 10 SASFCGSPYS ″ B*5801 76 ″ 12 6 ″ ″ 168 176 9 ASFCGSPYS 243 B*5802 19 ″ 3 6 ″ ″ 167 177 11 SASFCGSPYSW 244 B*5301 79 1,90 150 6 ″ ″ 167 177 11 SASFCGSPYSW ″ B*5701 94 ″ 179 6 ″ ″ 167 177 11 SASFCGSPYSW ″ B*5801 100 ″ 190 6 ″ ″ 167 177 11 SASFCGSPYSW ″ B*5802 100 ″ 190 6 ″ ″ 168 177 10 ASFCGSPYSW 245 B*4402 69 ″ 132 6 ″ ″ 168 177 10 ASFCGSPYSW ″ B*4403 28 ″ 53 6 ″ ″ 168 177 10 ASFCGSPYSW ″ B*5802 99 ″ 188 6 ″ ″ 169 177 9 SFCGSPYSW 246 A*2301 26 ″ 49 6 ″ ″ Cumulative Class I-BCI score: 10432 137 147 11 DQVVNHYFQTR 191 A*3303 21 1,63 34 7 137 170 138 147 10 QVVNHYFQTR 192 A*3101 1 ″ 2 7 ″ ″ 138 147 10 QVVNHYFQTR ″ A*3303 86 ″ 140 7 ″ ″ 138 147 10 QVVNHYFQTR ″ A*6801 68 ″ 110 7 ″ ″ 138 147 10 QVVNHYFQTR ″ A*7401 17 ″ 28 7 ″ ″ 139 147 9 VVNHYFQTR 193 A*3101 87 ″ 143 7 ″ ″ 139 147 9 VVNHYFQTR ″ A*3303 73 ″ 120 7 ″ ″ 139 147 9 VVNHYFQTR ″ A*7401 72 ″ 117 7 ″ ″ 139 149 11 VVNHYFQTRHY 194 A*0101 42 1,90 79 7 ″ ″ 139 149 11 VVNHYFQTRHY ″ A*2902 70 ″ 133 7 ″ ″ 139 149 11 VVNHYFQTRHY ″ A*3002 90 ″ 172 7 ″ ″ 139 149 11 VVNHYFQTRHY ″ B*1501 50 ″ 95 7 ″ ″ 139 149 11 VVNHYFQTRHY ″ B*1502 44 ″ 85 7 ″ ″ 141 149 9 NHYFQTRHY 195 B*3801 16 ″ 31 7 ″ ″ 142 149 8 HYFQTRHY 196 A*2902 25 ″ 48 7 ″ ″ 142 149 8 HYFQTRHY ″ A*3002 44 ″ 83 7 ″ ″ 141 150 10 NHYFQTRHYL 197 B*1402 94 1,93 181 7 ″ ″ 141 150 10 NHYFQTRHYL ″ B*3801 53 ″ 102 7 ″ ″ 141 150 10 NHYFQTRHYL ″ B*3901 88 ″ 170 7 ″ ″ 142 150 9 HYFQTRHYL 198 A*2301 69 ″ 133 7 ″ ″ 142 150 9 HYFQTRHYL ″ B*1402 34 ″ 66 7 ″ ″ 142 150 9 HYFQTRHYL ″ B*3901 3 ″ 5 7 ″ ″ 143 150 8 YFQTRHYL 199 A*2301 74 ″ 143 7 ″ ″ 143 150 8 YFQTRHYL ″ A*2402 74 ″ 142 7 ″ ″ 143 150 8 YFQTRHYL ″ B*0801 93 ″ 180 7 ″ ″ 142 151 10 HYFQTRHYLH 200 A*2301 33 0,39 13 7 ″ ″ 142 151 10 HYFQTRHYLH ″ A*2402 49 ″ 19 7 ″ ″ 142 151 10 HYFQTRHYLH ″ A*2902 16 ″ 6 7 ″ ″ 143 151 9 YFQTRHYLH 201 A*2902 57 ″ 22 7 ″ ″ 143 153 11 YFQTRHYLHTL 202 A*2301 98 1,22 120 7 ″ ″ 143 153 11 YFQTRHYLHTL ″ A*2402 100 ″ 122 7 ″ ″ 143 153 11 YFQTRHYLHTL ″ B*0801 100 ″ 122 7 ″ ″ 144 153 10 FQTRhYLHTL 203 A*0201 27 ″ 33 7 ″ ″ 144 153 10 FQTRHYLHTL ″ B*1301 63 ″ 77 7 ″ ″ 144 153 10 FQTRHYLHTL ″ B*1402 52 ″ 63 7 ″ ″ 144 153 10 FQTRHYLHTL ″ B*3701 62 ″ 75 7 ″ ″ 144 153 10 FQTRHYLHTL ″ B*3801 71 ″ 87 7 ″ ″ 144 153 10 FQTRHYLHTL ″ B*3901 94 ″ 114 7 ″ ″ 144 153 10 FQTRHYLHTL ″ B*4801 81 ″ 98 7 ″ ″ 145 153 9 QTRHYLHTL 204 A*2501 65 ″ 79 7 ″ ″ 146 153 8 TRHYLHTL 205 B*1402 72 ″ 87 7 ″ ″ 146 153 8 TRHYLHTL ″ B*2702 60 ″ 73 7 ″ ″ 146 153 8 TRHYLHTL ″ B*2705 70 ″ 85 7 ″ ″ 144 154 11 FQTRHYLHTLW 206 B*1301 68 1,50 101 7 ″ ″ 144 154 11 FQTRHYLHTLW ″ B*2702 37 ″ 56 7 ″ ″ 145 154 10 QTRHYLHTLW 207 B*4402 35 ″ 52 7 ″ ″ 145 154 10 QTRHYLHTLW ″ B*5802 70 ″ 104 7 ″ ″ 146 154 9 TRHYLHTLW 208 B*2702 76 ″ 114 7 ″ ″ 147 154 8 RHYLHTLW 209 A*2301 47 ″ 70 7 ″ ″ 147 154 8 RHYLHTLW ″ A*2402 35 ″ 52 7 ″ ″ 147 154 8 RHYLHTLW ″ B*2702 99 ″ 148 7 ″ ″ 147 154 8 RHYLHTLW ″ B*3801 98 ″ 147 7 ″ ″ 147 154 8 RHYLHTLW ″ B*5701 35 ″ 52 7 ″ ″ 147 154 8 RHYLHTLW ″ B*5801 22 ″ 33 7 ″ ″ 147 154 8 RHYLHTLW ″ B*5802 26 ″ 39 7 ″ ″ 145 155 11 QTRHYLHTLWK 210 A*0301 54 0,72 39 7 ″ ″ 145 155 11 QTRHYLHTLWK ″ A*1101 35 ″ 25 7 ″ ″ 145 155 11 QTRHYLHTLWK ″ A*3001 96 ″ 69 7 ″ ″ 146 155 10 TRHYLHTLWK 211 B*2705 36 ″ 26 7 ″ ″ 147 155 9 RHYLHTLWK 212 A*0301 70 ″ 51 7 ″ ″ 147 155 9 RHYLHTLWK ″ B*2702 7 ″ 5 7 ″ ″ 148 155 8 HYLHTLWK 213 A*3101 29 ″ 21 7 ″ ″ 146 156 11 TRHYLHTLWKA 214 B*2705 58 1,23 72 7 ″ ″ 148 156 9 HYLHTLWKA 215 A*2301 31 ″ 38 7 ″ ″ 147 157 11 RHYLHTLWKAG 216 B*2705 6 0,73 4 7 ″ ″ 148 157 10 HYLHTLWKAG 217 A*3201 74 ″ 54 7 ″ ″ 148 158 11 HYLHTLWKAGI 218 A*2301 93 0,63 59 7 ″ ″ 148 158 11 HYLHTLWKAGI ″ A*2402 95 ″ 60 7 ″ ″ 149 158 10 YLHTLWKAGI 219 A*0201 7 ″ 4 7 ″ ″ 151 158 8 HTLWKAGI 220 A*3201 62 ″ 39 7 ″ ″ 149 159 11 YLHTLWKAGIL 221 B*0801 88 0,85 75 7 ″ ″ 149 159 11 YLHTLWKAGIL ″ B*3901 22 ″ 19 7 ″ ″ 150 159 10 LHTLWKAGIL 222 B*0801 69 ″ 59 7 ″ ″ 150 159 10 LHTLWKAGIL ″ B*3801 51 ″ 43 7 ″ ″ 150 159 10 LHTLWKAGIL ″ B*3901 34 ″ 29 7 ″ ″ 151 159 9 HTLWKAGIL 223 B*5802 1 ″ 1 7 ″ ″ 151 160 10 HTLWKAGILY 224 A*0101 72 1,87 134 7 ″ ″ 151 160 10 HTLWKAGILY ″ A*0301 7 ″ 12 7 ″ ″ 151 160 10 HTLWKAGILY ″ A*2501 47 ″ 88 7 ″ ″ 151 160 10 HTLWKAGILY ″ A*2601 67 ″ 125 7 ″ ″ 151 160 10 HTLWKAGILY ″ A*2902 2 ″ 3 7 ″ ″ 151 160 10 HTLWKAGILY ″ A*3002 49 ″ 92 7 ″ ″ 152 160 9 TLWKAGILY 225 A*0301 36 ″ 67 7 ″ ″ 152 160 9 TLWKAGILY ″ A*2902 78 ″ 145 7 ″ ″ 152 160 9 TLWKAGILY ″ A*3002 4 ″ 8 7 ″ ″ 153 160 8 LWKAGILY 226 A*2902 56 ″ 104 7 ″ ″ 153 160 8 LWKAGILY ″ A*3002 85 ″ 158 7 ″ ″ 153 160 8 LWKAGILY ″ B*3501 8 ″ 15 7 ″ ″ 151 161 11 HTLWKAGILYK 227 A*0301 89 1,41 125 7 ″ ″ 151 161 11 HTLWKAGILYK ″ A*1101 100 ″ 141 7 ″ ″ 151 161 11 HTLWKAGILYK ″ A*3001 78 ″ 110 7 ″ ″ 151 161 11 HTLWKAGILYK ″ A*3101 46 ″ 64 7 ″ ″ 151 161 11 HTLWKAGILYK ″ A*3303 25 ″ 36 7 ″ ″ 151 161 11 HTLWKAGILYK ″ A*6801 75 ″ 106 7 ″ ″ 151 161 11 HTLWKAGILYK ″ A*7401 83 ″ 117 7 ″ ″ 152 161 10 TLWKAGILYK 228 A*0301 87 ″ 122 7 ″ ″ 152 161 10 TLWKAGILYK ″ A*1101 59 ″ 83 7 ″ ″ 152 161 10 TLWKAGILYK ″ A*7401 71 ″ 100 7 ″ ″ 153 161 9 LWKAGILYK 229 A*3001 57 ″ 80 7 ″ ″ 152 162 11 TLWKAGILYKR 230 A*3101 61 1,49 91 7 ″ ″ 152 162 11 TLWKAGILYKR ″ A*3303 72 ″ 107 7 ″ ″ 152 162 11 TLWKAGILYKR ″ A*7401 82 ″ 122 7 ″ ″ 153 162 10 LWKAGILYKR 231 A*3101 86 ″ 128 7 ″ ″ 153 162 10 LWKAGILYKR ″ A*3303 59 ″ 88 7 ″ ″ 155 162 8 KAGILYKR 232 A*3101 67 ″ 100 7 ″ ″ 155 162 8 KAGILYKR ″ A*7401 27 ″ 40 7 ″ ″ 158 166 9 ILYKRETTR 233 A*0301 66 1,75 115 7 ″ ″ 158 166 9 ILYKRETTR ″ A*3101 23 ″ 40 7 ″ ″ 158 166 9 ILYKRETTR ″ A*3303 51 ″ 89 7 ″ ″ 158 166 9 ILYKRETTR ″ A*7401 90 ″ 158 7 ″ ″ 158 168 11 ILYKRETTRSA 234 B*0801 56 1,80 100 7 ″ ″ 160 170 11 YKRETTRSASF 235 B*0702 17 1,82 32 7 ″ ″ 160 170 11 YKRETTRSASF ″ B*0801 81 ″ 148 7 ″ ″ 160 170 11 YKRETTRSASF ″ B*1402 68 ″ 123 7 ″ ″ 160 170 11 YKRETTRSASF ″ B*1501 53 ″ 97 7 ″ ″ 160 170 11 YKRETTRSASF ″ B*1502 65 ″ 118 7 ″ ″ 160 170 11 YKRETTRSASF ″ B*1525 46 ″ 83 7 ″ ″ 161 170 10 KRETTRSASF 236 B*2702 53 ″ 97 7 ″ ″ 162 170 9 RETTRSASF 237 B*4001 57 ″ 103 7 ″ ″ 162 170 9 RETTRSASF ″ B*4402 88 ″ 161 7 ″ ″ 162 170 9 RETTRSASF ″ B*4403 60 ″ 109 7 ″ ″ 162 170 9 RETTRSASF ″ B*5001 44 ″ 80 7 ″ ″ 163 170 8 ETTRSASF 238 A*2501 100 ″ 182 7 ″ ″ 163 170 8 ETTRSASF ″ A*2601 100 ″ 182 7 ″ ″ Cumulative Class I-BCI score: 10325 316 326 11 SQSQGSVSSCW 247 B*4402 46 1,49 69 8 316 347 316 326 11 SQSQGSVSSCW ″ B*4403 24 ″ 36 8 ″ ″ 317 326 10 QSQGSVSSCW 248 B*4402 54 ″ 80 8 ″ ″ 317 326 10 QSQGSVSSCW ″ B*5802 64 ″ 95 8 ″ ″ 319 326 8 QGSYSSCW 249 B*5801 15 ″ 23 8 ″ ″ 317 327 11 QSQGSVSSCWW 250 B*5701 79 1,02 80 8 ″ ″ 317 327 11 QSQGSVSSCWW ″ B*5801 88 ″ 90 8 ″ ″ 317 327 11 QSQGSVSSCWW ″ B*5802 75 ″ 77 8 ″ ″ 319 327 9 QGSYSSCWW 251 B*5701 38 ″ 39 8 ″ ″ 319 327 9 QGSYSSCWW ″ B*5801 10 ″ 10 8 ″ ″ 320 327 8 GSYSSCWW 252 B*5701 92 ″ 94 8 ″ ″ 320 327 8 GSYSSCWW ″ B*5801 95 ″ 97 8 ″ ″ 320 327 8 GSYSSCWW ″ B*5802 84 ″ 86 8 ″ ″ 318 328 11 SQGSVSSCWWL 253 B*4801 37 1,77 65 8 ″ ″ 320 329 10 GSYSSCWWLQ 254 A*3201 21 0,81 17 8 ″ ″ 320 330 11 GSVSSCWWLQF 255 B*1525 22 1,91 42 8 ″ ″ 320 330 11 GSVSSCWWLQF ″ B*5701 74 ″ 142 8 ″ ″ 320 330 11 GSVSSCWWLQF ″ B*5802 65 ″ 125 8 ″ ″ 321 330 10 SVSSCWWLQF 256 A*2601 31 ″ 59 8 ″ ″ 321 330 10 SVSSCWWLQF ″ A*3201 58 ″ 110 8 ″ ″ 322 330 9 VSSCWWLQF 257 A*0101 53 ″ 101 8 ″ ″ 322 330 9 VSSCWWLQF ″ A*2402 23 ″ 44 8 ″ ″ 322 330 9 VSSCWWLQF ″ B*4601 21 ″ 41 8 ″ ″ 322 330 9 VSSCWWLQF ″ B*5701 58 ″ 110 8 ″ ″ 322 330 9 VSSCWWLQF ″ B*5801 73 ″ 139 8 ″ ″ 323 330 8 SSCWWLQF 258 A*2301 21 ″ 40 8 ″ ″ 323 330 8 SSCWWLQF ″ A*3201 42 ″ 81 8 ″ ″ 323 330 8 SSCWWLQF ″ B*5801 59 ″ 113 8 ″ ″ 321 331 11 SYSSCWWLQFR 259 A*1101 65 0,81 53 8 ″ ″ 321 331 11 SYSSCWWLQFR ″ A*3303 100 ″ 81 8 ″ ″ 321 331 11 SYSSCWWLQFR ″ A*6801 96 ″ 78 8 ″ ″ 321 331 11 SYSSCWWLQFR ″ A*7401 98 ″ 79 8 ″ ″ 322 331 10 VSSCWWLQFR 260 A*3101 95 ″ 77 8 ″ ″ 322 331 10 VSSCWWLQFR ″ A*3303 56 ″ 46 8 ″ ″ 322 331 10 VSSCWWLQFR ″ B*5701 30 ″ 25 8 ″ ″ 322 331 10 VSSCWWLQFR ″ B*5801 42 ″ 34 8 ″ ″ 323 331 9 SSCWWLQFR 261 A*1101 41 ″ 34 8 ″ ″ 323 331 9 SSCWWLQFR ″ A*3101 94 ″ 76 8 ″ ″ 323 331 9 SSCWWLQFR ″ A*3303 85 ″ 69 8 ″ ″ 323 331 9 SSCWWLQFR ″ A*7401 87 ″ 70 8 ″ ″ 324 331 8 SCWWLQFR 262 A*3303 44 ″ 36 8 ″ ″ 327 334 8 WLQFRNSK 263 A*0301 20 0,52 10 8 ″ ″ 328 335 8 LQFRNSKP 264 A*0206 21 0,10 2 8 ″ ″ 327 336 10 WLQFRNSKPC 265 A*0201 18 0,14 3 8 ″ ″ 328 337 10 LQFRNSKPCS 266 A*3001 99 0,26 26 8 ″ ″ 329 339 11 QFRNSKPCSEY 267 A*3002 10 1,63 16 8 ″ ″ 331 339 9 RNSKPCSEY 268 A*3002 8 ″ 14 8 ″ ″ 332 339 8 NSKPCSEY 269 A*3002 20 ″ 32 8 ″ ″ 336 343 8 CSEYCLSH 270 A*0101 40 0,58 23 8 ″ ″ 337 344 8 SEYCLSHL 271 B*1301 97 1,01 98 8 ″ ″ 337 344 8 SEYCLSHL ″ B*1302 37 ″ 37 8 ″ ″ 337 344 8 SEYCLSHL ″ B*1801 67 ″ 67 8 ″ ″ 337 344 8 SEYCLSHL ″ B*3701 100 ″ 101 8 ″ ″ 337 344 8 SEYCLSHL ″ B*3801 96 ″ 97 8 ″ ″ 337 344 8 SEYCLSHL ″ B*4001 100 ″ 101 8 ″ ″ 337 344 8 SEYCLSHL ″ B*4002 100 ″ 101 8 ″ ″ 337 344 8 SEYCLSHL ″ B*4402 85 ″ 85 8 ″ ″ 337 344 8 SEYCLSHL ″ B*4403 88 ″ 89 8 ″ ″ 337 344 8 SEYCLSHL ″ B*4801 46 ″ 47 8 ″ ″ 337 344 8 SEYCLSHL ″ B*4901 96 ″ 97 8 ″ ″ 337 344 8 SEYCLSHL ″ B*5001 96 ″ 97 8 ″ ″ 337 344 8 SEYCLSHL ″ B*5201 57 ″ 57 8 ″ ″ 335 345 11 PCSEYCLSHLV 272 A*0201 40 1,78 71 8 ″ ″ 337 345 9 SEYCLSHLV 273 B*1301 94 ″ 168 8 ″ ″ 337 345 9 SEYCLSHLV ″ B*1302 48 ″ 85 8 ″ ″ 337 345 9 SEYCLSHLV ″ B*1801 29 ″ 51 8 ″ ″ 337 345 9 SEYCLSHLV ″ B*4001 65 ″ 116 8 ″ ″ 337 345 9 SEYCLSHLV ″ B*4002 70 ″ 125 8 ″ ″ 337 345 9 SEYCLSHLV ″ B*4402 77 ″ 137 8 ″ ″ 337 345 9 SEYCLSHLV ″ B*4403 80 ″ 142 8 ″ ″ 337 345 9 SEYCLSHLV ″ B*4901 100 ″ 178 8 ″ ″ 337 345 9 SEYCLSHLV ″ B*5001 100 ″ 178 8 ″ ″ 337 345 9 SEYCLSHLV ″ B*5201 71 ″ 126 8 ″ ″ 337 346 10 SEYCLSHLVN 274 B*4001 39 0,24 10 8 ″ ″ 337 346 10 SEYCLSHLVN ″ B*4403 76 ″ 18 8 ″ ″ 337 346 10 SEYCLSHLVN ″ B*5001 24 ″ 6 8 ″ ″ 337 347 11 SEYCLSHLVNL 275 B*1301 100 1,66 166 8 ″ ″ 337 347 11 SEYCLSHLVNL ″ B*1302 45 ″ 75 8 ″ ″ 337 347 11 SEYCLSHLVNL ″ B*1801 86 ″ 142 8 ″ ″ 337 347 11 SEYCLSHLVNL ″ B*3701 95 ″ 158 8 ″ ″ 337 347 11 SEYCLSHLVNL ″ B*3801 94 ″ 156 8 ″ ″ 337 347 11 SEYCLSHLVNL ″ B*4001 96 ″ 158 8 ″ ″ 337 347 11 SEYCLSHLVNL ″ B*4002 95 ″ 157 8 ″ ″ 337 347 11 SEYCLSHLVNL ″ B*4402 81 ″ 134 8 ″ ″ 337 347 11 SEYCLSHLVNL ″ B*4403 84 ″ 139 8 ″ ″ 337 347 11 SEYCLSHLVNL ″ B*4901 91 ″ 151 8 ″ ″ 337 347 11 SEYCLSHLVNL ″ B*5001 92 ″ 152 8 ″ ″ 337 347 11 SEYCLSHLVNL ″ B*5201 63 ″ 104 8 ″ ″ 338 347 10 EYCLSHLVNL 276 A*2301 48 ″ 80 8 ″ ″ Cumulative Class I-BCI score: 7246 386 394 9 AESRLVVDF 278 B*1801 10 1,80 17 9 385 417 386 394 9 AESRLVVDF ″ B*4001 48 ″ 86 9 ″ ″ 386 394 9 AESRLVVDF ″ B*4002 50 ″ 90 9 ″ ″ 386 394 9 AESRLVVDF ″ B*4402 100 ″ 180 9 ″ ″ 386 394 9 AESRLVVDF ″ B*4403 100 ″ 180 9 ″ ″ 386 394 9 AESRLVVDF ″ B*4901 43 ″ 78 9 ″ ″ 386 394 9 AESRLVVDF ″ B*5001 36 ″ 65 9 ″ ″ 386 396 11 AESRLVVDFSQ 279 B*4402 15 0,65 10 9 ″ ″ 386 396 11 AESRLVVDFSQ ″ B*4403 8 ″ 5 9 ″ ″ 387 397 11 ESRLVVDFSQF 280 A*2501 49 1,86 91 9 ″ ″ 387 397 11 ESRLVVDFSQF ″ A*2601 5 ″ 10 9 ″ ″ 388 397 10 SRLVVDFSQF 281 B*2702 92 ″ 170 9 ″ ″ 389 397 9 RLVVDFSQF 282 A*2301 43 ″ 80 9 ″ ″ 389 397 9 RLVVDFSQF ″ B*1501 70 ″ 131 9 ″ ″ 389 397 9 RLVVDFSQF ″ B*1525 78 ″ 145 9 ″ ″ 390 397 8 LVVDFSQF 283 A*2501 59 ″ 110 9 ″ ″ 390 397 8 LVVDFSQF ″ A*2601 79 ″ 148 9 ″ ″ 390 397 8 LVVDFSQF ″ B*1501 59 ″ 110 9 ″ ″ 390 397 8 LVVDFSQF ″ B*1502 72 ″ 134 9 ″ ″ 390 397 8 LVVDFSQF ″ B*1525 56 ″ 104 9 ″ ″ 390 397 8 LVVDFSQF ″ B*4601 57 ″ 107 9 ″ ″ 389 399 11 RLVVDFSQFSR 284 A*0301 15 1,78 26 9 ″ ″ 389 399 11 RLVVDFSQFSR ″ A*3101 81 ″ 144 9 ″ ″ 389 399 11 RLVVDFSQFSR ″ A*7401 96 ″ 172 9 ″ ″ 390 399 10 LVVDFSQFSR 285 A*3101 89 ″ 158 9 ″ ″ 390 399 10 LVVDFSQFSR ″ A*3201 6 ″ 11 9 ″ ″ 390 399 10 LVVDFSQFSR ″ A*3303 83 ″ 148 9 ″ ″ 390 399 10 LVVDFSQFSR ″ A*6801 88 ″ 157 9 ″ ″ 390 399 10 LVVDFSQFSR ″ A*7401 70 ″ 124 9 ″ ″ 391 399 9 VVDFSQFSR 286 A*1101 11 ″ 19 9 ″ ″ 391 399 9 VVDFSQFSR ″ A*3303 18 ″ 33 9 ″ ″ 391 399 9 VVDFSQFSR ″ A*7401 79 ″ 141 9 ″ ″ 390 400 11 LVVDFSQFSRG 287 A*6802 6 0,16 1 9 ″ ″ 392 401 10 VDFSQFSRGI 288 B*1301 76 1,23 93 9 ″ ″ 392 401 10 VDFSQFSRGI ″ B*1302 44 ″ 54 9 ″ ″ 392 401 10 VDFSQFSRGI ″ B*5201 88 ″ 108 9 ″ ″ 393 403 11 DFSQFSRGISR 289 A*3303 55 0,77 42 9 ″ ″ 394 403 10 FSQFSRGISR 290 A*3101 14 ″ 11 9 ″ ″ 394 403 10 FSQFSRGISR ″ A*3303 11 ″ 9 9 ″ ″ 394 403 10 FSQFSRGISR ″ A*6801 60 ″ 46 9 ″ ″ 395 403 9 SQFSRGISR 291 A*1101 13 ″ 10 9 ″ ″ 395 403 9 SQFSRGISR ″ A*3101 62 ″ 48 9 ″ ″ 395 403 9 SQFSRGISR ″ A*3303 70 ″ 54 9 ″ ″ 395 403 9 SQFSRGISR ″ A*7401 95 ″ 73 9 ″ ″ 396 403 8 QFSRGISR 292 A*3303 48 ″ 37 9 ″ ″ 395 404 10 SQFSrGISRV 293 A*0201 45 1,90 85 9 ″ ″ 395 404 10 SQFSRGISRV ″ B*1302 23 ″ 43 9 ″ ″ 395 404 10 SQFSRGISRV ″ B*1402 4 ″ 8 9 ″ ″ 395 404 10 SQFSRGISRV ″ B*3901 27 ″ 52 9 ″ ″ 395 404 10 SQFSRGISRV ″ B*4801 35 ″ 66 9 ″ ″ 395 404 10 SQFSRGISRV ″ B*5201 69 ″ 130 9 ″ ″ 398 405 8 sRGISRVS 294 B*2705 12 0,22 3 9 ″ ″ 397 406 10 FSRGISRVSW 295 B*4601 38 1,40 53 9 ″ ″ 397 406 10 FSRGISRVSW ″ B*5301 15 ″ 21 9 ″ ″ 397 406 10 FSRGISRVSW ″ B*5802 87 ″ 122 9 ″ ″ 398 406 9 SRGISRVSW 296 B*2702 65 ″ 91 9 ″ ″ 399 406 8 RGISRVSW 297 B*2702 28 ″ 39 9 ″ ″ 399 406 8 RGISRVSW ″ B*5701 73 ″ 102 9 ″ ″ 399 406 8 RGISRVSW ″ B*5801 68 ″ 95 9 ″ ″ 399 406 8 RGISRVSW ″ B*5802 74 ″ 103 9 ″ ″ 400 408 9 GISRVSWPK 298 A*0301 62 0,98 61 9 ″ ″ 400 408 9 GISRVSWPK ″ A*1101 93 ″ 91 9 ″ ″ 400 408 9 GISRVSWPK ″ A*7401 40 ″ 39 9 ″ ″ 401 408 8 ISRVSWPK 299 A*0301 13 ″ 13 9 ″ ″ 401 408 8 ISRVSWPK ″ A*1101 30 ″ 30 9 ″ ″ 401 408 8 ISRVSWPK ″ A*3001 95 ″ 92 9 ″ ″ 399 409 11 RGISRVSWPKF 300 A*2301 7 1,38 10 9 ″ ″ 399 409 11 RGISRVSWPKF ″ B*5802 7 ″ 10 9 ″ ″ 400 409 10 GISRVSWPKF 301 A*3001 55 ″ 77 9 ″ ″ 400 409 10 GISRVSWPKF ″ A*3201 98 ″ 136 9 ″ ″ 401 409 9 ISRVSWPKF 302 B*5701 88 ″ 122 9 ″ ″ 402 409 8 sRvswpKF 303 B*2702 90 ″ 125 9 ″ ″ 402 409 8 sRvswpKF ″ B*2705 57 ″ 78 9 ″ ″ 403 410 8 RVSWPKFA 304 A*3001 16 0,84 14 9 ″ ″ 401 411 11 ISRVSWPKFAV 305 A*3001 70 1,60 111 9 ″ ″ 402 411 10 SRVSWPKFAV 306 B*3901 6 ″ 10 9 ″ ″ 403 411 9 RVSWPKFAV 307 A*6802 4 ″ 7 9 ″ ″ 403 411 9 RVSWPKFAV ″ B*0702 6 ″ 9 9 ″ ″ 404 411 8 VSWPKFAV 308 B*5201 41 ″ 66 9 ″ ″ 405 412 8 SWPKFAVP 309 A*0206 100 0,48 48 9 ″ ″ 404 414 11 VSWPKFAVPNL 310 B*5201 16 1,63 26 9 ″ ″ 404 414 11 VSWPKFAVPNL ″ B*5701 18 ″ 30 9 ″ ″ 405 414 10 SWPKFAVPNL 311 A*2301 78 ″ 127 9 ″ ″ 405 414 10 SWPKFAVPNL ″ A*2402 75 ″ 123 9 ″ ″ 406 414 9 WPKFAVPNL 312 B*1402 21 ″ 35 9 ″ ″ 406 414 9 WPKFAVPNL ″ B*3503 18 ″ 29 9 ″ ″ 409 417 9 FAVPNLQSL 313 A*0206 54 1,89 102 9 ″ ″ 409 417 9 FAVPNLQSL ″ B*3503 46 ″ 87 9 ″ ″ 409 417 9 FAVPNLQSL ″ B*4601 95 ″ 180 9 ″ ″ 410 417 8 AVPNLQSL 314 B*0702 29 ″ 55 9 ″ ″ Cumulative BCI Class Iscore: 6722 420 427 8 LLSSNLSW 316 B*5301 20 1,77 35 10 419 456 420 427 8 LLSSNLSW ″ B*5701 48 ″ 86 10 ″ ″ 420 427 8 LLSSNLSW ″ B*5801 66 ″ 117 10 ″ ″ 420 427 8 LLSSNLSW ″ B*5802 30 ″ 54 10 ″ ″ 419 428 10 NLLSsNLSWL 317 A*0201 100 1,54 154 10 ″ ″ 420 428 9 LLSSNLSWL 318 A*0201 86 ″ 133 10 ″ ″ 421 428 8 LSSNLSWL 319 B*0702 78 ″ 121 10 ″ ″ 421 429 9 LSSNLSWLS 320 A*0101 30 0,55 16 10 ″ ″ 420 430 11 LLSSNLSWLSL 321 B*0801 8 1,74 15 10 ″ ″ 421 430 10 LSSNLSWLSL 322 A*3201 47 ″ 82 10 ″ ″ 421 430 10 LSSNLSWLSL ″ B*5701 27 ″ 48 10 ″ ″ 421 430 10 LSSNLSWLSL ″ B*5801 3 ″ 6 10 ″ ″ 421 430 10 LSSNLSWLSL ″ B*5802 29 ″ 50 10 ″ ″ 422 431 10 SSNLSWLSLD 323 A*3001 22 0,11 2 10 ″ ″ 422 432 11 SSNLSWLSLDV 324 A*0201 38 1,41 53 10 ″ ″ 424 432 9 NLSWLSLDV 325 A*0201 29 ″ 41 10 ″ ″ 425 432 8 LSWLSLDV 326 A*0206 4 ″ 6 10 ″ ″ 425 432 8 LSWLSLDV ″ B*1302 1 ″ 2 10 ″ ″ 425 432 8 LSWLSLDV ″ B*5201 55 ″ 77 10 ″ ″ 425 435 11 LSWLSLDVSAA 327 B*5601 9 0,74 7 10 ″ ″ 427 435 9 WLSLDVSAA 328 A*0201 14 ″ 10 10 ″ ″ 426 436 11 SWLSLDVSAAF 329 A*2301 91 1,90 174 10 ″ ″ 426 436 11 SWLSLDVSAAF ″ A*2402 93 ″ 177 10 ″ ″ 426 436 11 SWLSLDVSAAF ″ A*2902 32 ″ 60 10 ″ ″ 426 436 11 SWLSLDVSAAF ″ B*1801 38 ″ 72 10 ″ ″ 427 436 10 WLSLDVSAAF 330 B*1501 72 ″ 137 10 ″ ″ 427 436 10 WLSLDVSAAF ″ B*1502 89 ″ 169 10 ″ ″ 427 436 10 WLSLDVSAAF ″ B*1525 54 ″ 103 10 ″ ″ 428 436 9 LSLDVSAAF 331 B*1501 73 ″ 140 10 ″ ″ 428 436 9 LSLDVSAAF ″ B*1525 76 ″ 145 10 ″ ″ 428 436 9 LSLDVSAAF ″ B*3501 69 ″ 132 10 ″ ″ 428 436 9 LSLDVSAAF ″ B*3503 51 ″ 98 10 ″ ″ 428 436 9 LSLDVSAAF ″ B*4601 75 ″ 144 10 ″ ″ 428 436 9 LSLDVSAAF ″ B*5801 63 ″ 119 10 ″ ″ 427 437 11 WLSLDVSAAFY 332 A*0101 74 1,81 133 10 ″ ″ 427 437 11 WLSLDVSAAFY ″ A*2601 38 ″ 69 10 ″ ″ 427 437 11 WLSLDVSAAFY ″ A*2902 75 ″ 135 10 ″ ″ 427 437 11 WLSLDVSAAFY ″ B*1502 22 ″ 40 10 ″ ″ 428 437 10 LSLDVSAAFY 333 A*0101 100 ″ 181 10 ″ ″ 428 437 10 LSLDVSAAFY ″ A*2902 83 ″ 149 10 ″ ″ 428 437 10 LSLDVSAAFY ″ A*3002 99 ″ 178 10 ″ ″ 428 437 10 LSLDVSAAFY ″ B*1501 22 ″ 40 10 ″ ″ 428 437 10 LSLDVSAAFY ″ B*4601 69 ″ 124 10 ″ ″ 428 437 10 LSLDVSAAFY ″ B*5802 57 ″ 102 10 ″ ″ 429 437 9 SLDVSAAFY 334 A*0101 85 ″ 153 10 ″ ″ 429 437 9 SLDVSAAFY ″ A*3002 59 ″ 107 10 ″ ″ 430 437 8 LDVSAAFY 335 B*3501 31 ″ 55 10 ″ ″ 430 439 10 LDVSAAFYHI 336 B*1301 96 1,79 171 10 ″ ″ 430 439 10 LDVSAAFYHI ″ B*1302 49 ″ 88 10 ″ ″ 430 439 10 LDVSAAFYHI ″ B*3701 57 ″ 102 10 ″ ″ 430 439 10 LDVSAAFYHI ″ B*4901 57 ″ 101 10 ″ ″ 430 439 10 LDVSAAFYHI ″ B*5201 98 ″ 175 10 ″ ″ 431 439 9 DVSAAFYHI 337 A*6802 46 ″ 81 10 ″ ″ 432 439 8 VSAAFYHI 338 A*3201 18 ″ 32 10 ″ ″ 432 439 8 VSAAFYHI ″ B*1302 28 ″ 50 10 ″ ″ 432 439 8 VSAAFYHI ″ B*5101 8 ″ 15 10 ″ ″ 432 439 8 VSAAFYHI ″ B*5201 96 ″ 172 10 ″ ″ 432 439 8 VSAAFYHI ″ B*5701 65 ″ 116 10 ″ ″ 432 439 8 VSAAFYHI ″ B*5801 64 ″ 115 10 ″ ″ 432 439 8 VSAAFYHI ″ B*5802 49 ″ 88 10 ″ ″ 431 441 11 DVSAAFYHIPL 339 A*2501 33 1,00 33 10 ″ ″ 431 441 11 DVSAAFYHIPL ″ A*2601 51 ″ 51 10 ″ ″ 432 441 10 VSAAFYHIPL 340 A*6802 35 ″ 35 10 ″ ″ 432 441 10 VSAAFYHIPL ″ B*5802 14 ″ 15 10 ″ ″ 433 441 9 SAAFYHIPL 341 B*1402 79 ″ 79 10 ″ ″ 433 441 9 SAAFYHIPL ″ B*3503 34 ″ 34 10 ″ ″ 434 441 8 AAFYHIPL 342 B*0801 64 ″ 65 10 ″ ″ 434 441 8 AAFYHIPL ″ B*1402 57 ″ 57 10 ″ ″ 434 441 8 AAFYHIPL ″ B*3801 6 ″ 6 10 ″ ″ 434 441 8 AAFYHIPL ″ B*3901 32 ″ 33 10 ″ ″ 434 441 8 AAFYHIPL ″ B*4801 63 ″ 64 10 ″ ″ 433 442 10 SAAFYHIPLH 343 A*3001 83 0,25 20 10 ″ ″ 434 444 11 AAFYHIPLHPA 344 A*3001 11 0,89 10 10 ″ ″ 434 444 11 AAFYHIPLHPA ″ B*5501 20 ″ 18 10 ″ ″ 434 444 11 AAFYHIPLHPA ″ B*5601 21 ″ 18 10 ″ ″ 437 444 8 YHIPLHPA 345 B*1402 19 ″ 17 10 ″ ″ 437 444 8 YHIPLHPA ″ B*3901 87 ″ 78 10 ″ ″ 437 445 9 YHIPLHPAA 346 B*1402 18 0,62 11 10 ″ ″ 436 446 11 FYHIPLHPAAM 347 A*2402 19 1,63 31 10 ″ ″ 437 446 10 YHIPLHPAAM 348 B*1402 99 ″ 161 10 ″ ″ 437 446 10 YHIPLHPAAM ″ B*3503 74 ″ 121 10 ″ ″ 437 446 10 YHIPLHPAAM ″ B*3801 86 ″ 140 10 ″ ″ 437 446 10 YHIPLHPAAM ″ B*3901 100 ″ 163 10 ″ ″ 438 446 9 HIPLHPAAM 349 A*2501 73 ″ 120 10 ″ ″ 438 446 9 HIPLHPAAM ″ B*1402 3 ″ 5 10 ″ ″ 439 446 8 IPLHPAAM 350 B*1402 86 ″ 140 10 ″ ″ 439 446 8 IPLHPAAM ″ B*3503 93 ″ 152 10 ″ ″ 439 446 8 IPLHPAAM ″ B*5101 55 ″ 90 10 ″ ″ 439 446 8 IPLHPAAM ″ B*5301 64 ″ 104 10 ″ ″ 439 446 8 IPLHPAAM ″ B*5501 85 ″ 138 10 ″ ″ 439 446 8 IPLHPAAM ″ B*5601 73 ″ 119 10 ″ ″ 439 449 11 IPLHPAAMPHL 351 B*0702 58 1,61 93 10 ″ ″ 439 449 11 IPLHPAAMPHL ″ B*1402 31 ″ 50 10 ″ ″ 439 449 11 IPLHPAAMPHL ″ B*3503 32 ″ 52 10 ″ ″ 439 449 11 IPLHPAAMPHL ″ B*5101 53 ″ 86 10 ″ ″ 439 449 11 IPLHPAAMPHL ″ B*5501 38 ″ 62 10 ″ ″ 441 449 9 LHPAAMPHL 352 B*3801 76 ″ 121 10 ″ ″ 442 449 8 HPAAMPHL 353 B*1402 85 ″ 136 10 ″ ″ 442 449 8 HPAAMPHL ″ B*3503 73 ″ 117 10 ″ ″ 442 449 8 HPAAMPHL ″ B*3901 53 ″ 85 10 ″ ″ 442 449 8 HPAAMPHL ″ B*5101 48 ″ 78 10 ″ ″ 442 449 8 HPAAMPHL ″ B*5301 38 ″ 61 10 ″ ″ 442 449 8 HPAAMPHL ″ B*5501 55 ″ 88 10 ″ ″ 442 449 8 HPAAMPHL ″ B*5601 29 ″ 47 10 ″ ″ 441 450 10 LHPAAMPHLL 354 B*3801 67 1,81 122 10 ″ ″ 442 450 9 HPAAMPHLL 355 B*0702 70 ″ 126 10 ″ ″ 442 450 9 HPAAMPHLL ″ B*1402 93 ″ 168 10 ″ ″ 442 450 9 HPAAMPHLL ″ B*3501 29 ″ 53 10 ″ ″ 442 450 9 HPAAMPHLL ″ B*3503 85 ″ 154 10 ″ ″ 442 450 9 HPAAMPHLL ″ B*3901 97 ″ 176 10 ″ ″ 442 450 9 HPAAMPHLL ″ B*5301 33 ″ 59 10 ″ ″ 442 450 9 HPAAMPHLL ″ B*5501 72 ″ 130 10 ″ ″ 442 450 9 HPAAMPHLL ″ B*5601 58 ″ 104 10 ″ ″ 441 451 11 LHPAAMPHLLI 356 B*3801 61 0,84 51 10 ″ ″ 442 451 10 HPAAMPHLLI 357 B*1402 71 ″ 59 10 ″ ″ 442 451 10 HPAAMPHLLI ″ B*3503 72 ″ 60 10 ″ ″ 442 451 10 HPAAMPHLLI ″ B*3901 38 ″ 31 10 ″ ″ 442 451 10 HPAAMPHLLI ″ B*5201 61 ″ 51 10 ″ ″ 442 451 10 HPAAMPHLLI ″ B*5301 36 ″ 30 10 ″ ″ 442 451 10 HPAAMPHLLI ″ B*5501 84 ″ 70 10 ″ ″ 442 451 10 HPAAMPHLLI ″ B*5601 90 ″ 75 10 ″ ″ 444 451 8 AAMPHLLI 358 A*3201 59 ″ 49 10 ″ ″ 444 451 8 AAMPHLLI ″ B*1302 35 ″ 29 10 ″ ″ 444 451 8 AAMPHLLI ″ B*5101 47 ″ 39 10 ″ ″ 444 451 8 AAMPHLLI ″ B*5201 94 ″ 79 10 ″ ″ 444 451 8 AAMPHLLI ″ B*5801 37 ″ 31 10 ″ ″ 442 452 11 HPAAMPHLLIG 359 A*0201 51 0,32 16 10 ″ ″ 442 452 11 HPAAMPHLLIG ″ A*0206 38 ″ 12 10 ″ ″ 446 453 8 MPHLLIGS 360 A*6802 16 0,77 12 10 ″ ″ 446 453 8 MPHLLIGS ″ B*5601 28 ″ 22 10 ″ ″ 446 454 9 MPHLLIGSS 361 B*5501 37 0,26 10 10 ″ ″ 446 454 9 MPHLLIGSS ″ B*5601 41 ″ 11 10 ″ ″ 446 455 10 MPHLLIGSSG 362 B*0702 35 0,11 4 10 ″ ″ 446 455 10 MPHLLIGSSG ″ B*3501 40 ″ 4 10 ″ ″ 446 455 10 MPHLLIGSSG ″ B*5501 3 ″ 0 10 ″ ″ 446 455 10 MPHLLIGSSG ″ B*5601 18 ″ 2 10 ″ ″ 446 456 11 MPHLLIGSSGL 363 B*0702 93 1,81 168 10 ″ ″ 446 456 11 MPHLLIGSSGL ″ B*0801 44 ″ 80 10 ″ ″ 446 456 11 MPHLLIGSSGL ″ B*1402 92 ″ 167 10 ″ ″ 446 456 11 MPHLLIGSSGL ″ B*3501 27 ″ 48 10 ″ ″ 446 456 11 MPHLLIGSSGL ″ B*3503 70 ″ 127 10 ″ ″ 446 456 11 MPHLLIGSSGL ″ B*3901 62 ″ 113 10 ″ ″ 446 456 11 MPHLLIGSSGL ″ B*5101 40 ″ 73 10 ″ ″ 446 456 11 MPHLLIGSSGL ″ B*5301 18 ″ 33 10 ″ ″ 446 456 11 MPHLLIGSSGL ″ B*5501 71 ″ 129 10 ″ ″ 446 456 11 MPHLLIGSSGL ″ B*5601 53 ″ 95 10 ″ ″ 448 456 9 HLLIGSSGL 364 B*1502 83 ″ 151 10 ″ ″ 449 456 8 LLIGSSGL 365 B*0702 77 ″ 139 10 ″ ″ Cumulative BCI Class Iscore: 11926 422 432 11 SSNLSWLSLDV 324 A*0201 38 1,41 53 11 422 459 424 432 9 NLSWLSLDV 325 A*0201 29 ″ 41 11 ″ ″ 425 432 8 LSWLSLDV 326 A*0206 4 ″ 6 11 ″ ″ 425 432 8 LSWLSLDV ″ B*1302 1 ″ 2 11 ″ ″ 425 432 8 LSWLSLDV ″ B*5201 55 ″ 77 11 ″ ″ 425 435 11 LSWLSLDVSAA 327 B*5601 9 0,74 7 11 ″ ″ 427 435 9 WLSLDVSAA 328 A*0201 14 ″ 10 11 ″ ″ 426 436 11 SWLSLDVSAAF 329 A*2301 91 1,90 174 11 ″ ″ 426 436 11 SWLSLDVSAAF ″ A*2402 93 ″ 177 11 ″ ″ 426 436 11 SWLSLDVSAAF ″ A*2902 32 ″ 60 11 ″ ″ 426 436 11 SWLSLDVSAAF ″ B*1801 38 ″ 72 11 ″ ″ 427 436 10 WLSLDVSAAF 330 B*1501 72 ″ 137 11 ″ ″ 427 436 10 WLSLDVSAAF ″ B*1502 89 ″ 169 11 ″ ″ 427 436 10 WLSLDVSAAF ″ B*1525 54 ″ 103 11 ″ ″ 428 436 9 LSLDVSAAF 331 B*1501 73 ″ 140 11 ″ ″ 428 436 9 LSLDVSAAF ″ B*1525 76 ″ 145 11 ″ ″ 428 436 9 LSLDVSAAF ″ B*3501 69 ″ 132 11 ″ ″ 428 436 9 LSLDVSAAF ″ B*3503 51 ″ 98 11 ″ ″ 428 436 9 LSLDVSAAF ″ B*4601 75 ″ 144 11 ″ ″ 428 436 9 LSLDVSAAF ″ B*5801 63 ″ 119 11 ″ ″ 427 437 11 WLSLDVSAAFY 332 A*0101 74 1,81 133 11 ″ ″ 427 437 11 WLSLDVSAAFY ″ A*2601 38 ″ 69 11 ″ ″ 427 437 11 WLSLDVSAAFY ″ A*2902 75 ″ 135 11 ″ ″ 427 437 11 WLSLDVSAAFY ″ B*1502 22 ″ 40 11 ″ ″ 428 437 10 LSLDVSAAFY 333 A*0101 100 ″ 181 11 ″ ″ 428 437 10 LSLDVSAAFY ″ A*2902 83 ″ 149 11 ″ ″ 428 437 10 LSLDVSAAFY ″ A*3002 99 ″ 178 11 ″ ″ 428 437 10 LSLDVSAAFY ″ B*1501 22 ″ 40 11 ″ ″ 428 437 10 LSLDVSAAFY ″ B*4601 69 ″ 124 11 ″ ″ 428 437 10 LSLDVSAAFY ″ B*5802 57 ″ 102 11 ″ ″ 429 437 9 SLDVSAAFY 334 A*0101 85 ″ 153 11 ″ ″ 429 437 9 SLDVSAAFY ″ A*3002 59 ″ 107 11 ″ ″ 430 437 8 LDVSAAFY 335 B*3501 31 ″ 55 11 ″ ″ 430 439 10 LDVSAAFYHI 336 B*1301 96 1,79 171 11 ″ ″ 430 439 10 LDVSAAFYHI ″ B*1302 49 ″ 88 11 ″ ″ 430 439 10 LDVSAAFYHI ″ B*3701 57 ″ 102 11 ″ ″ 430 439 10 LDVSAAFYHI ″ B*4901 57 ″ 101 11 ″ ″ 430 439 10 LDVSAAFYHI ″ B*5201 98 ″ 175 11 ″ ″ 431 439 9 DVSAAFYHI 337 A*6802 46 ″ 81 11 ″ ″ 432 439 8 VSAAFYHI 338 A*3201 18 ″ 32 11 ″ ″ 432 439 8 VSAAFYHI ″ B*1302 28 ″ 50 11 ″ ″ 432 439 8 VSAAFYHI ″ B*5101 8 ″ 15 11 ″ ″ 432 439 8 VSAAFYHI ″ B*5201 96 ″ 172 11 ″ ″ 432 439 8 VSAAFYHI ″ B*5701 65 ″ 116 11 ″ ″ 432 439 8 VSAAFYHI ″ B*5801 64 ″ 115 11 ″ ″ 432 439 8 VSAAFYHI ″ B*5802 49 ″ 88 11 ″ ″ 431 441 11 DVSAAFYHIPL 339 A*2501 33 1,00 33 11 ″ ″ 431 441 11 DVSAAFYHIPL ″ A*2601 51 ″ 51 11 ″ ″ 432 441 10 VSAAFYHIPL 340 A*6802 35 ″ 35 11 ″ ″ 432 441 10 VSAAFYHIPL ″ B*5802 14 ″ 15 11 ″ ″ 433 441 9 SAAFYHIPL 341 B*1402 79 ″ 79 11 ″ ″ 433 441 9 SAAFYHIPL ″ B*3503 34 ″ 34 11 ″ ″ 434 441 8 AAFYHIPL 342 B*0801 64 ″ 65 11 ″ ″ 434 441 8 AAFYHIPL ″ B*1402 57 ″ 57 11 ″ ″ 434 441 8 AAFYHIPL ″ B*3801 6 ″ 6 11 ″ ″ 434 441 8 AAFYHIPL ″ B*3901 32 ″ 33 11 ″ ″ 434 441 8 AAFYHIPL ″ B*4801 63 ″ 64 11 ″ ″ 433 442 10 SAAFYHIPLH 343 A*3001 83 0,25 20 11 ″ ″ 434 444 11 AAFYHIPLHPA 344 A*3001 11 0,89 10 11 ″ ″ 434 444 11 AAFYHIPLHPA ″ B*5501 20 ″ 18 11 ″ ″ 434 444 11 AAFYHIPLHPA ″ B*5601 21 ″ 18 11 ″ ″ 437 444 8 YHIPLHPA 345 B*1402 19 ″ 17 11 ″ ″ 437 444 8 YHIPLHPA ″ B*3901 87 ″ 78 11 ″ ″ 437 445 9 YHIPLHPAA 346 B*1402 18 0,62 11 11 ″ ″ 436 446 11 FYHIPLHPAAM 347 A*2402 19 1,63 31 11 ″ ″ 437 446 10 YHIPLHPAAM 348 B*1402 99 ″ 161 11 ″ ″ 437 446 10 YHIPLHPAAM ″ B*3503 74 ″ 121 11 ″ ″ 437 446 10 YHIPLHPAAM ″ B*3801 86 ″ 140 11 ″ ″ 437 446 10 YHIPLHPAAM ″ B*3901 100 ″ 163 11 ″ ″ 438 446 9 HIPLHPAAM 349 A*2501 73 ″ 120 11 ″ ″ 438 446 9 HIPLHPAAM ″ B*1402 3 ″ 5 11 ″ ″ 439 446 8 IPLHPAAM 350 B*1402 86 ″ 140 11 ″ ″ 439 446 8 IPLHPAAM ″ B*3503 93 ″ 152 11 ″ ″ 439 446 8 IPLHPAAM ″ B*5101 55 ″ 90 11 ″ ″ 439 446 8 IPLHPAAM ″ B*5301 64 ″ 104 11 ″ ″ 439 446 8 IPLHPAAM ″ B*5501 85 ″ 138 11 ″ ″ 439 446 8 IPLHPAAM ″ B*5601 73 ″ 119 11 ″ ″ 439 449 11 IPLHPAAMPHL 351 B*0702 58 1,61 93 11 ″ ″ 439 449 11 IPLHPAAMPHL ″ B*1402 31 ″ 50 11 ″ ″ 439 449 11 IPLHPAAMPHL ″ B*3503 32 ″ 52 11 ″ ″ 439 449 11 IPLHPAAMPHL ″ B*5101 53 ″ 86 11 ″ ″ 439 449 11 IPLHPAAMPHL ″ B*5501 38 ″ 62 11 ″ ″ 441 449 9 LHPAAMPHL 352 B*3801 76 ″ 121 11 ″ ″ 442 449 8 HPAAMPHL 353 B*1402 85 ″ 136 11 ″ ″ 442 449 8 HPAAMPHL ″ B*3503 73 ″ 117 11 ″ ″ 442 449 8 HPAAMPHL ″ B*3901 53 ″ 85 11 ″ ″ 442 449 8 HPAAMPHL ″ B*5101 48 ″ 78 11 ″ ″ 442 449 8 HPAAMPHL ″ B*5301 38 ″ 61 11 ″ ″ 442 449 8 HPAAMPHL ″ B*5501 55 ″ 88 11 ″ ″ 442 449 8 HPAAMPHL ″ B*5601 29 ″ 47 11 ″ ″ 441 450 10 LHPAAMPHLL 354 B*3801 67 1,81 122 11 ″ ″ 442 450 9 HPAAMPHLL 355 B*0702 70 ″ 126 11 ″ ″ 442 450 9 HPAAMPHLL ″ B*1402 93 ″ 168 11 ″ ″ 442 450 9 HPAAMPHLL ″ B*3501 29 ″ 53 11 ″ ″ 442 450 9 HPAAMPHLL ″ B*3503 85 ″ 154 11 ″ ″ 442 450 9 HPAAMPHLL ″ B*3901 97 ″ 176 11 ″ ″ 442 450 9 HPAAMPHLL ″ B*5301 33 ″ 59 11 ″ ″ 442 450 9 HPAAMPHLL ″ B*5501 72 ″ 130 11 ″ ″ 442 450 9 HPAAMPHLL ″ B*5601 58 ″ 104 11 ″ ″ 441 451 11 LHPAAMPHLLI 356 B*3801 61 0,84 51 11 ″ ″ 442 451 10 HPAAMPHLLI 357 B*1402 71 ″ 59 11 ″ ″ 442 451 10 HPAAMPHLLI ″ B*3503 72 ″ 60 11 ″ ″ 442 451 10 HPAAMPHLLI ″ B*3901 38 ″ 31 11 ″ ″ 442 451 10 HPAAMPHLLI ″ B*5201 61 ″ 51 11 ″ ″ 442 451 10 HPAAMPHLLI ″ B*5301 36 ″ 30 11 ″ ″ 442 451 10 HPAAMPHLLI ″ B*5501 84 ″ 70 11 ″ ″ 442 451 10 HPAAMPHLLI ″ B*5601 90 ″ 75 11 ″ ″ 444 451 8 AAMPHLLI 358 A*3201 59 ″ 49 11 ″ ″ 444 451 8 AAMPHLLI ″ B*1302 35 ″ 29 11 ″ ″ 444 451 8 AAMPHLLI ″ B*5101 47 ″ 39 11 ″ ″ 444 451 8 AAMPHLLI ″ B*5201 94 ″ 79 11 ″ ″ 444 451 8 AAMPHLLI ″ B*5801 37 ″ 31 11 ″ ″ 442 452 11 HPAAMPHLLIG 359 A*0201 51 0,32 16 11 ″ ″ 442 452 11 HPAAMPHLLIG ″ A*0206 38 ″ 12 11 ″ ″ 446 453 8 MPHLLIGS 360 A*6802 16 0,77 12 11 ″ ″ 446 453 8 MPHLLIGS ″ B*5601 28 ″ 22 11 ″ ″ 446 454 9 MPHLLIGSS 361 B*5501 37 0,26 10 11 ″ ″ 446 454 9 MPHLLIGSS ″ B*5601 41 ″ 11 11 ″ ″ 446 455 10 MPHLLIGSSG 362 B*0702 35 0,11 4 11 ″ ″ 446 455 10 MPHLLIGSSG ″ B*3501 40 ″ 4 11 ″ ″ 446 455 10 MPHLLIGSSG ″ B*5501 3 ″ 0 11 ″ ″ 446 455 10 MPHLLIGSSG ″ B*5601 18 ″ 2 11 ″ ″ 446 456 11 MPHLLIGSSGL 363 B*0702 93 1,81 168 11 ″ ″ 446 456 11 MPHLLIGSSGL ″ B*0801 44 ″ 80 11 ″ ″ 446 456 11 MPHLLIGSSGL ″ B*1402 92 ″ 167 11 ″ ″ 446 456 11 MPHLLIGSSGL ″ B*3501 27 ″ 48 11 ″ ″ 446 456 11 MPHLLIGSSGL ″ B*3503 70 ″ 127 11 ″ ″ 446 456 11 MPHLLIGSSGL ″ B*3901 62 ″ 113 11 ″ ″ 446 456 11 MPHLLIGSSGL ″ B*5101 40 ″ 73 11 ″ ″ 446 456 11 MPHLLIGSSGL ″ B*5301 18 ″ 33 11 ″ ″ 446 456 11 MPHLLIGSSGL ″ B*5501 71 ″ 129 11 ″ ″ 446 456 11 MPHLLIGSSGL ″ B*5601 53 ″ 95 11 ″ ″ 448 456 9 HLLIGSSGL 364 B*1502 83 ″ 151 11 ″ ″ 449 456 8 LLIGSSGL 365 B*0702 77 ″ 139 11 ″ ″ 448 458 11 HLLIGSSGLSR 366 A*0301 11 1,14 13 11 ″ ″ 448 458 11 HLLIGSSGLSR ″ A*3101 19 ″ 22 11 ″ ″ 448 458 11 HLLIGSSGLSR ″ A*3303 17 ″ 19 11 ″ ″ 448 458 11 HLLIGSSGLSR ″ A*7401 62 ″ 71 11 ″ ″ 449 458 10 LLIGSSGLSR 367 A*7401 6 ″ 7 11 ″ ″ 449 459 11 LLIGSSGLSRY 368 A*2501 57 1,50 85 11 ″ ″ 449 459 11 LLIGSSGLSRY ″ A*2601 77 ″ 115 11 ″ ″ 449 459 11 LLIGSSGLSRY ″ A*2902 89 ″ 133 11 ″ ″ 449 459 11 LLIGSSGLSRY ″ A*3002 66 ″ 99 11 ″ ″ 449 459 11 LLIGSSGLSRY ″ B*1501 81 ″ 122 11 ″ ″ 449 459 11 LLIGSSGLSRY ″ B*1502 57 ″ 86 11 ″ ″ 449 459 11 LLIGSSGLSRY ″ B*1525 41 ″ 61 11 ″ ″ 449 459 11 LLIGSSGLSRY ″ B*4601 28 ″ 42 11 ″ ″ 450 459 10 LIGSSGLSRY 369 A*0101 45 ″ 68 11 ″ ″ 450 459 10 LIGSSGLSRY ″ A*3002 35 ″ 53 11 ″ ″ 451 459 9 IGSSGLSRY 370 A*3002 94 ″ 141 11 ″ ″ 452 459 8 GSSGLSRY 371 A*0101 83 ″ 124 11 ″ ″ 452 459 8 GSSGLSRY ″ A*3002 77 ″ 116 11 ″ ″ Cumulative Class I-BCI score: 12384 427 435 9 WLSLDVSAA 328 A*0201 14 0,74 10 12 427 459 426 436 11 SWLSLDVSAAF 329 A*2301 91 1,90 174 12 ″ ″ 426 436 11 SWLSLDVSAAF ″ A*2402 93 ″ 177 12 ″ ″ 426 436 11 SWLSLDVSAAF ″ A*2902 32 ″ 60 12 ″ ″ 426 436 11 SWLSLDVSAAF ″ B*1801 38 ″ 72 12 ″ ″ 427 436 10 WLSLDVSAAF 330 B*1501 72 ″ 137 12 ″ ″ 427 436 10 WLSLDVSAAF ″ B*1502 89 ″ 169 12 ″ ″ 427 436 10 WLSLDVSAAF ″ B*1525 54 ″ 103 12 ″ ″ 428 436 9 LSLDVSAAF 331 B*1501 73 ″ 140 12 ″ ″ 428 436 9 LSLDVSAAF ″ B*1525 76 ″ 145 12 ″ ″ 428 436 9 LSLDVSAAF ″ B*3501 69 ″ 132 12 ″ ″ 428 436 9 LSLDVSAAF ″ B*3503 51 ″ 98 12 ″ ″ 428 436 9 LSLDVSAAF ″ B*4601 75 ″ 144 12 ″ ″ 428 436 9 LSLDVSAAF ″ B*5801 63 ″ 119 12 ″ ″ 427 437 11 WLSLDVSAAFY 332 A*0101 74 1,81 133 12 ″ ″ 427 437 11 WLSLDVSAAFY ″ A*2601 38 ″ 69 12 ″ ″ 427 437 11 WLSLDVSAAFY ″ A*2902 75 ″ 135 12 ″ ″ 427 437 11 WLSLDVSAAFY ″ B*1502 22 ″ 40 12 ″ ″ 428 437 10 LSLDVSAAFY 333 A*0101 100 ″ 181 12 ″ ″ 428 437 10 LSLDVSAAFY ″ A*2902 83 ″ 149 12 ″ ″ 428 437 10 LSLDVSAAFY ″ A*3002 99 ″ 178 12 ″ ″ 428 437 10 LSLDVSAAFY ″ B*1501 22 ″ 40 12 ″ ″ 428 437 10 LSLDVSAAFY ″ B*4601 69 ″ 124 12 ″ ″ 428 437 10 LSLDVSAAFY ″ B*5802 57 ″ 102 12 ″ ″ 429 437 9 SLDVSAAFY 334 A*0101 85 ″ 153 12 ″ ″ 429 437 9 SLDVSAAFY ″ A*3002 59 ″ 107 12 ″ ″ 430 437 8 LDVSAAFY 335 B*3501 31 ″ 55 12 ″ ″ 430 439 10 LDVSAAFYHI 336 B*1301 96 1,79 171 12 ″ ″ 430 439 10 LDVSAAFYHI ″ B*1302 49 ″ 88 12 ″ ″ 430 439 10 LDVSAAFYHI ″ B*3701 57 ″ 102 12 ″ ″ 430 439 10 LDVSAAFYHI ″ B*4901 57 ″ 101 12 ″ ″ 430 439 10 LDVSAAFYHI ″ B*5201 98 ″ 175 12 ″ ″ 431 439 9 DVSAAFYHI 337 A*6802 46 ″ 81 12 ″ ″ 432 439 8 VSAAFYHI 338 A*3201 18 ″ 32 12 ″ ″ 432 439 8 VSAAFYHI ″ B*1302 28 ″ 50 12 ″ ″ 432 439 8 VSAAFYHI ″ B*5101 8 ″ 15 12 ″ ″ 432 439 8 VSAAFYHI ″ B*5201 96 ″ 172 12 ″ ″ 432 439 8 VSAAFYHI ″ B*5701 65 ″ 116 12 ″ ″ 432 439 8 VSAAFYHI ″ B*5801 64 ″ 115 12 ″ ″ 432 439 8 VSAAFYHI ″ B*5802 49 ″ 88 12 ″ ″ 431 441 11 DVSAAFYHIPL 339 A*2501 33 1,00 33 12 ″ ″ 431 441 11 DVSAAFYHIPL ″ A*2601 51 ″ 51 12 ″ ″ 432 441 10 VSAAFYHIPL 340 A*6802 35 ″ 35 12 ″ ″ 432 441 10 VSAAFYHIPL ″ B*5802 14 ″ 15 12 ″ ″ 433 441 9 SAAFYHIPL 341 B*1402 79 ″ 79 12 ″ ″ 433 441 9 SAAFYHIPL ″ B*3503 34 ″ 34 12 ″ ″ 434 441 8 AAFYHIPL 342 B*0801 64 ″ 65 12 ″ ″ 434 441 8 AAFYHIPL ″ B*1402 57 ″ 57 12 ″ ″ 434 441 8 AAFYHIPL ″ B*3801 6 ″ 6 12 ″ ″ 434 441 8 AAFYHIPL ″ B*3901 32 ″ 33 12 ″ ″ 434 441 8 AAFYHIPL ″ B*4801 63 ″ 64 12 ″ ″ 433 442 10 SAAFYHIPLH 343 A*3001 83 0,25 20 12 ″ ″ 434 444 11 AAFYHIPLHPA 344 A*3001 11 0,89 10 12 ″ ″ 434 444 11 AAFYHIPLHPA ″ B*5501 20 ″ 18 12 ″ ″ 434 444 11 AAFYHIPLHPA ″ B*5601 21 ″ 18 12 ″ ″ 437 444 8 YHIPLHPA 345 B*1402 19 ″ 17 12 ″ ″ 437 444 8 YHIPLHPA ″ B*3901 87 ″ 78 12 ″ ″ 437 445 9 YHIPLHPAA 346 B*1402 18 0,62 11 12 ″ ″ 436 446 11 FYHIPLHPAAM 347 A*2402 19 1,63 31 12 ″ ″ 437 446 10 YHIPLHPAAM 348 B*1402 99 ″ 161 12 ″ ″ 437 446 10 YHIPLHPAAM ″ B*3503 74 ″ 121 12 ″ ″ 437 446 10 YHIPLHPAAM ″ B*3801 86 ″ 140 12 ″ ″ 437 446 10 YHIPLHPAAM ″ B*3901 100 ″ 163 12 ″ ″ 438 446 9 HIPLHPAAM 349 A*2501 73 ″ 120 12 ″ ″ 438 446 9 HIPLHPAAM ″ B*1402 3 ″ 5 12 ″ ″ 439 446 8 IPLHPAAM 350 B*1402 86 ″ 140 12 ″ ″ 439 446 8 IPLHPAAM ″ B*3503 93 ″ 152 12 ″ ″ 439 446 8 IPLHPAAM ″ B*5101 55 ″ 90 12 ″ ″ 439 446 8 IPLHPAAM ″ B*5301 64 ″ 104 12 ″ ″ 439 446 8 IPLHPAAM ″ B*5501 85 ″ 138 12 ″ ″ 439 446 8 IPLHPAAM ″ B*5601 73 ″ 119 12 ″ ″ 439 449 11 IPLHPAAMPHL 351 B*0702 58 1,61 93 12 ″ ″ 439 449 11 IPLHPAAMPHL ″ B*1402 31 ″ 50 12 ″ ″ 439 449 11 IPLHPAAMPHL ″ B*3503 32 ″ 52 12 ″ ″ 439 449 11 IPLHPAAMPHL ″ B*5101 53 ″ 86 12 ″ ″ 439 449 11 IPLHPAAMPHL ″ B*5501 38 ″ 62 12 ″ ″ 441 449 9 LHPAAMPHL 352 B*3801 76 ″ 121 12 ″ ″ 442 449 8 HPAAMPHL 353 B*1402 85 ″ 136 12 ″ ″ 442 449 8 HPAAMPHL ″ B*3503 73 ″ 117 12 ″ ″ 442 449 8 HPAAMPHL ″ B*3901 53 ″ 85 12 ″ ″ 442 449 8 HPAAMPHL ″ B*5101 48 ″ 78 12 ″ ″ 442 449 8 HPAAMPHL ″ B*5301 38 ″ 61 12 ″ ″ 442 449 8 HPAAMPHL ″ B*5501 55 ″ 88 12 ″ ″ 442 449 8 HPAAMPHL ″ B*5601 29 ″ 47 12 ″ ″ 441 450 10 LHPAAMPHLL 354 B*3801 67 1,81 122 12 ″ ″ 442 450 9 HPAAMPHLL 355 B*0702 70 ″ 126 12 ″ ″ 442 450 9 HPAAMPHLL ″ B*1402 93 ″ 168 12 ″ ″ 442 450 9 HPAAMPHLL ″ B*3501 29 ″ 53 12 ″ ″ 442 450 9 HPAAMPHLL ″ B*3503 85 ″ 154 12 ″ ″ 442 450 9 HPAAMPHLL ″ B*3901 97 ″ 176 12 ″ ″ 442 450 9 HPAAMPHLL ″ B*5301 33 ″ 59 12 ″ ″ 442 450 9 HPAAMPHLL ″ B*5501 72 ″ 130 12 ″ ″ 442 450 9 HPAAMPHLL ″ B*5601 58 ″ 104 12 ″ ″ 441 451 11 LHPAAMPHLLI 356 B*3801 61 0,84 51 12 ″ ″ 442 451 10 HPAAMPHLLI 357 B*1402 71 ″ 59 12 ″ ″ 442 451 10 HPAAMPHLLI ″ B*3503 72 ″ 60 12 ″ ″ 442 451 10 HPAAMPHLLI ″ B*3901 38 ″ 31 12 ″ ″ 442 451 10 HPAAMPHLLI ″ B*5201 61 ″ 51 12 ″ ″ 442 451 10 HPAAMPHLLI ″ B*5301 36 ″ 30 12 ″ ″ 442 451 10 HPAAMPHLLI ″ B*5501 84 ″ 70 12 ″ ″ 442 451 10 HPAAMPHLLI ″ B*5601 90 ″ 75 12 ″ ″ 444 451 8 AAMPHLLI 358 A*3201 59 ″ 49 12 ″ ″ 444 451 8 AAMPHLLI ″ B*1302 35 ″ 29 12 ″ ″ 444 451 8 AAMPHLLI ″ B*5101 47 ″ 39 12 ″ ″ 444 451 8 AAMPHLLI ″ B*5201 94 ″ 79 12 ″ ″ 444 451 8 AAMPHLLI ″ B*5801 37 ″ 31 12 ″ ″ 442 452 11 HPAAMPHLLIG 359 A*0201 51 0,32 16 12 ″ ″ 442 452 11 HPAAMPHLLIG ″ A*0206 38 ″ 12 12 ″ ″ 446 453 8 MPHLLIGS 360 A*6802 16 0,77 12 12 ″ ″ 446 453 8 MPHLLIGS ″ B*5601 28 ″ 22 12 ″ ″ 446 454 9 MPHLLIGSS 361 B*5501 37 0,26 10 12 ″ ″ 446 454 9 MPHLLIGSS ″ B*5601 41 ″ 11 12 ″ ″ 446 455 10 MPHLLIGSSG 362 B*0702 35 0,11 4 12 ″ ″ 446 455 10 MPHLLIGSSG ″ B*3501 40 ″ 4 12 ″ ″ 446 455 10 MPHLLIGSSG ″ B*5501 3 ″ 0 12 ″ ″ 446 455 10 MPHLLIGSSG ″ B*5601 18 ″ 2 12 ″ ″ 446 456 11 MPHLLIGSSGL 363 B*0702 93 1,81 168 12 ″ ″ 446 456 11 MPHLLIGSSGL ″ B*0801 44 ″ 80 12 ″ ″ 446 456 11 MPHLLIGSSGL ″ B*1402 92 ″ 167 12 ″ ″ 446 456 11 MPHLLIGSSGL ″ B*3501 27 ″ 48 12 ″ ″ 446 456 11 MPHLLIGSSGL ″ B*3503 70 ″ 127 12 ″ ″ 446 456 11 MPHLLIGSSGL ″ B*3901 62 ″ 113 12 ″ ″ 446 456 11 MPHLLIGSSGL ″ B*5101 40 ″ 73 12 ″ ″ 446 456 11 MPHLLIGSSGL ″ B*5301 18 ″ 33 12 ″ ″ 446 456 11 MPHLLIGSSGL ″ B*5501 71 ″ 129 12 ″ ″ 446 456 11 MPHLLIGSSGL ″ B*5601 53 ″ 95 12 ″ ″ 448 456 9 HLLIGSSGL 364 B*1502 83 ″ 151 12 ″ ″ 449 456 8 LLIGSSGL 365 B*0702 77 ″ 139 12 ″ ″ 448 458 11 HLLIGSSGLSR 366 A*0301 11 1,14 13 12 ″ ″ 448 458 11 HLLIGSSGLSR ″ A*3101 19 ″ 22 12 ″ ″ 448 458 11 HLLIGSSGLSR ″ A*3303 17 ″ 19 12 ″ ″ 448 458 11 HLLIGSSGLSR ″ A*7401 62 ″ 71 12 ″ ″ 449 458 10 LLIGSSGLSR 367 A*7401 6 ″ 7 12 ″ ″ 449 459 11 LLIGSSGLSRY 368 A*2501 57 1,50 85 12 ″ ″ 449 459 11 LLIGSSGLSRY ″ A*2601 77 ″ 115 12 ″ ″ 449 459 11 LLIGSSGLSRY ″ A*2902 89 ″ 133 12 ″ ″ 449 459 11 LLIGSSGLSRY ″ A*3002 66 ″ 99 12 ″ ″ 449 459 11 LLIGSSGLSRY ″ B*1501 81 ″ 122 12 ″ ″ 449 459 11 LLIGSSGLSRY ″ B*1502 57 ″ 86 12 ″ ″ 449 459 11 LLIGSSGLSRY ″ B*1525 41 ″ 61 12 ″ ″ 449 459 11 LLIGSSGLSRY ″ B*4601 28 ″ 42 12 ″ ″ 450 459 10 LIGSSGLSRY 369 A*0101 45 ″ 68 12 ″ ″ 450 459 10 LIGSSGLSRY ″ A*3002 35 ″ 53 12 ″ ″ 451 459 9 IGSSGLSRY 370 A*3002 94 ″ 141 12 ″ ″ 452 459 8 GSSGLSRY 371 A*0101 83 ″ 124 12 ″ ″ 452 459 8 GSSGLSRY ″ A*3002 77 ″ 116 12 ″ ″ Cumulative Class I-BCI score: 12198 485 492 8 SRQLYVSL 372 B*1402 84 1,59 134 13 481 514 485 492 8 SRQLYVSL ″ B*2702 89 ″ 142 13 ″ ″ 485 492 8 SRQLYVSL ″ B*3901 86 ″ 137 13 ″ ″ 485 492 8 SRQLYVSL ″ B*4801 2 ″ 3 13 ″ ″ 484 493 10 CSRQLYVSLM 373 B*4601 43 1,55 66 13 ″ ″ 485 493 9 SRQLYVSLM 374 B*2702 88 ″ 137 13 ″ ″ 485 493 9 SRQLYVSLM ″ B*2705 85 ″ 132 13 ″ ″ 486 493 8 RQLYVSLM 375 A*3201 53 ″ 82 13 ″ ″ 486 493 8 RQLYVSLM ″ B*1301 85 ″ 131 13 ″ ″ 486 493 8 RQLYVSLM ″ B*1302 13 ″ 20 13 ″ ″ 486 493 8 RQLYVSLM ″ B*1402 15 ″ 24 13 ″ ″ 486 493 8 RQLYVSLM ″ B*1501 48 ″ 75 13 ″ ″ 486 493 8 RQLYVSLM ″ B*1525 75 ″ 116 13 ″ ″ 486 493 8 RQLYVSLM ″ B*2702 73 ″ 114 13 ″ ″ 486 493 8 RQLYVSLM ″ B*3901 51 ″ 79 13 ″ ″ 486 493 8 RQLYVSLM ″ B*4801 94 ″ 146 13 ″ ″ 485 494 10 SRQLYVSLML 376 B*1402 49 1,55 77 13 ″ ″ 485 494 10 SRQLYVSLML ″ B*2702 87 ″ 135 13 ″ ″ 485 494 10 SRQLYVSLML ″ B*2705 88 ″ 137 13 ″ ″ 485 494 10 SRQLYVSLML ″ B*3901 52 ″ 81 13 ″ ″ 486 494 9 RQLYVSLML 377 A*0206 19 ″ 29 13 ″ ″ 486 494 9 RQLYVSLML ″ A*3201 79 ″ 122 13 ″ ″ 486 494 9 RQLYVSLML ″ B*1301 80 ″ 125 13 ″ ″ 486 494 9 RQLYVSLML ″ B*1302 21 ″ 33 13 ″ ″ 486 494 9 RQLYVSLML ″ B*2702 72 ″ 112 13 ″ ″ 486 494 9 RQLYVSLML ″ B*2705 52 ″ 81 13 ″ ″ 486 494 9 RQLYVSLML ″ B*4001 52 ″ 81 13 ″ ″ 486 494 9 RQLYVSLML ″ B*4801 96 ″ 149 13 ″ ″ 487 494 8 QLYVSLML 378 A*0201 58 ″ 90 13 ″ ″ 485 495 11 SRQLYVSLMLL 379 B*1402 16 1,34 22 13 ″ ″ 485 495 11 SRQLYVSLMLL ″ B*2702 98 ″ 131 13 ″ ″ 485 495 11 SRQLYVSLMLL ″ B*2705 25 ″ 34 13 ″ ″ 486 495 10 RQLYVSLMLL 380 A*0206 48 ″ 64 13 ″ ″ 486 495 10 RQLYVSLMLL ″ B*1301 87 ″ 117 13 ″ ″ 486 495 10 RQLYVSLMLL ″ B*1302 34 ″ 45 13 ″ ″ 486 495 10 RQLYVSLMLL ″ B*2702 86 ″ 115 13 ″ ″ 486 495 10 RQLYVSLMLL ″ B*3801 10 ″ 14 13 ″ ″ 486 495 10 RQLYVSLMLL ″ B*3901 43 ″ 57 13 ″ ″ 486 495 10 RQLYVSLMLL ″ B*4801 100 ″ 134 13 ″ ″ 488 495 8 LYVSLMLL 381 A*2301 72 ″ 97 13 ″ ″ 488 495 8 LYVSLMLL ″ A*2402 72 ″ 96 13 ″ ″ 488 495 8 LYVSLMLL ″ B*0702 91 ″ 122 13 ″ ″ 486 496 11 RQLYVSLMLLY 382 A*0301 61 1,80 109 13 ″ ″ 486 496 11 RQLYVSLMLLY ″ B*1501 47 ″ 84 13 ″ ″ 486 496 11 RQLYVSLMLLY ″ B*1525 68 ″ 122 13 ″ ″ 486 496 11 RQLYVSLMLLY ″ B*2702 84 ″ 152 13 ″ ″ 486 496 11 RQLYVSLMLLY ″ B*2705 76 ″ 137 13 ″ ″ 487 496 10 QLYVSLMLLY 383 B*4403 44 ″ 79 13 ″ ″ 488 496 9 LYVSLMLLY 384 A*2902 98 ″ 177 13 ″ ″ 489 496 8 YVSLMLLY 385 A*0101 94 ″ 170 13 ″ ″ 489 496 8 YVSLMLLY ″ A*2501 90 ″ 162 13 ″ ″ 489 496 8 YVSLMLLY ″ A*2601 97 ″ 176 13 ″ ″ 489 496 8 YVSLMLLY ″ A*3002 87 ″ 157 13 ″ ″ 489 496 8 YVSLMLLY ″ B*3501 88 ″ 159 13 ″ ″ 489 496 8 YVSLMLLY ″ B*4601 56 ″ 100 13 ″ ″ 487 497 11 QLYVSLMLLYK 386 A*1101 85 1,07 91 13 ″ ″ 487 497 11 QLYVSLMLLYK ″ A*7401 61 ″ 65 13 ″ ″ 488 497 10 LYVSLMLLYK 387 A*0301 25 ″ 26 13 ″ ″ 489 497 9 YVSLMLLYK 388 A*0301 67 ″ 72 13 ″ ″ 489 497 9 YVSLMLLYK ″ A*1101 91 ″ 98 13 ″ ″ 489 497 9 YVSLMLLYK ″ A*6801 66 ″ 71 13 ″ ″ 489 497 9 YVSLMLLYK ″ A*7401 12 ″ 13 13 ″ ″ 490 497 8 VSLMLLYK 389 A*0301 80 ″ 86 13 ″ ″ 490 497 8 VSLMLLYK ″ A*1101 98 ″ 105 13 ″ ″ 490 497 8 VSLMLLYK ″ A*7401 35 ″ 38 13 ″ ″ 489 499 11 YVSLMLLYKTY 390 A*0101 81 1,86 151 13 ″ ″ 489 499 11 YVSLMLLYKTY ″ A*2501 55 ″ 102 13 ″ ″ 489 499 11 YVSLMLLYKTY ″ A*2601 74 ″ 138 13 ″ ″ 489 499 11 YvsLMLLYKTY ″ A*2902 86 ″ 159 13 ″ ″ 489 499 11 YvsLMLLYKTY ″ A*3002 42 ″ 78 13 ″ ″ 489 499 11 YvsLMLLYKTY ″ B*1502 31 ″ 58 13 ″ ″ 489 499 11 YvsLMLLYKTY ″ B*4601 13 ″ 24 13 ″ ″ 490 499 10 VSUALYKTY 391 A*0101 75 ″ 140 13 ″ ″ 490 499 10 VSUALYKTY ″ A*3002 48 ″ 89 13 ″ ″ 490 499 10 VSUALYKTY ″ B*5802 38 ″ 70 13 ″ ″ 492 499 8 LMLLYKTY 392 A*2902 52 ″ 97 13 ″ ″ 492 499 8 LMLLYKTY ″ B*1525 19 ″ 35 13 ″ ″ 492 499 8 LMLLYKTY ″ B*3501 57 ″ 106 13 ″ ″ 491 500 10 SLMLLYKTYG 393 A*0201 9 0,13 1 13 ″ ″ 491 501 11 SLMLLYKTYGW 394 A*3201 68 1,93 132 13 ″ ″ 492 501 10 LMLLYKTYGW 395 A*2301 17 ″ 33 13 ″ ″ 492 501 10 LMLLYKTYGW ″ B*5301 28 ″ 54 13 ″ ″ 492 501 10 LMLLYKTYGW ″ B*5802 36 ″ 70 13 ″ ″ 493 501 9 MLLYKTYGW 396 A*3201 92 ″ 179 13 ″ ″ 493 501 9 MLLYKTYGW ″ B*5701 36 ″ 70 13 ″ ″ 493 501 9 MLLYKTYGW ″ B*5801 31 ″ 59 13 ″ ″ 494 501 8 LLYKTYGW 397 A*3201 50 ″ 97 13 ″ ″ 494 501 8 LLYKTYGW ″ B*5701 47 ″ 91 13 ″ ″ 494 501 8 LLYKTYGW ″ B*5801 53 ″ 102 13 ″ ″ 494 501 8 LLYKTYGW ″ B*5802 6 ″ 11 13 ″ ″ 492 502 11 LMLLYKTYGWK 398 A*0206 15 0,71 10 13 ″ ″ 492 502 11 LMLLYKTYGWK ″ A*0301 79 ″ 56 13 ″ ″ 492 502 11 LMLLYKTYGWK ″ A*1101 20 ″ 14 13 ″ ″ 492 502 11 LMLLYKTYGWK ″ A*7401 34 ″ 24 13 ″ ″ 493 502 10 MLLYKTYGWK 399 A*0301 97 ″ 69 13 ″ ″ 493 502 10 MLLYKTYGWK ″ A*1101 26 ″ 19 13 ″ ″ 493 502 10 MLLYKTYGWK ″ A*7401 48 ″ 34 13 ″ ″ 494 502 9 LLYKTYGWK 400 A*0301 95 ″ 68 13 ″ ″ 495 502 8 LYKTYGWK 401 A*3001 24 ″ 17 13 ″ ″ 493 503 11 MLLYKTYGWKL 402 A*3201 52 ″ 100 13 ″ ″ 493 503 11 MLLYKTYGWKL ″ B*0801 98 ″ 192 13 ″ ″ 493 503 11 MLLYKTYGWKL ″ B*1402 9 ″ 18 13 ″ ″ 494 503 10 LLYKtYGWKL 403 A*0201 82 ″ 58 13 ″ ″ 495 503 9 LYKTYGWKL 404 A*2301 24 1,95 47 13 ″ ″ 495 503 9 LYKTYGWKL ″ A*2402 60 ″ 116 13 ″ ″ 496 503 8 YKTYGWKL 405 B*3901 84 ″ 165 13 ″ ″ 495 504 10 LYKTYGWKLH 406 A*3201 35 0,88 31 13 ″ ″ 497 504 8 KTYGWKLH 407 A*0301 59 ″ 52 13 ″ ″ 497 504 8 KTYGWKLH ″ A*7401 5 ″ 4 13 ″ ″ 495 505 11 LYKTYGWKLHL 408 A*2301 45 1,71 77 13 ″ ″ 495 505 11 LYKTYGWKLHL ″ A*2402 51 ″ 87 13 ″ ″ 496 505 10 YKTYGWKLHL 409 B*3901 12 ″ 20 13 ″ ″ 497 505 9 KTYGWKLHL 410 A*3201 86 ″ 148 13 ″ ″ 497 505 9 KTYGWKLHL ″ A*7401 4 ″ 6 13 ″ ″ 497 505 9 KTYGWKLHL ″ B*5701 68 ″ 117 13 ″ ″ 497 505 9 KTYGWKLHL ″ B*5801 47 ″ 81 13 ″ ″ 497 505 9 KTYGWKLHL ″ B*5802 28 ″ 47 13 ″ ″ 498 505 8 TYGWKLHL 411 A*2301 64 ″ 109 13 ″ ″ 498 505 8 TYGWKLHL ″ A*2402 63 ″ 108 13 ″ ″ 496 506 11 YKTYGWKLHLY 412 A*2902 30 1,90 57 13 ″ ″ 497 506 10 KTYGWKLHLY 413 A*0101 77 ″ 147 13 ″ ″ 497 506 10 KTYGWKLHLY ″ A*0301 92 ″ 175 13 ″ ″ 497 506 10 KTYGWKLHLY ″ A*2501 78 ″ 148 13 ″ ″ 497 506 10 KTYGWKLHLY ″ A*3002 97 ″ 185 13 ″ ″ 497 506 10 KTYGWKLHLY ″ A*7401 85 ″ 162 13 ″ ″ 497 506 10 KTYGWKLHLY ″ B*5802 83 ″ 157 13 ″ ″ 498 506 9 TYGWKLHLY 414 A*2402 37 ″ 70 13 ″ ″ 498 506 9 TYGWKLHLY ″ A*2902 90 ″ 172 13 ″ ″ 498 506 9 TYGWKLHLY ″ A*3002 70 ″ 134 13 ″ ″ 499 506 8 YGWKLHLY 415 A*2902 97 ″ 184 13 ″ ″ 499 506 8 YGWKLHLY ″ A*3002 76 ″ 145 13 ″ ″ 499 506 8 YGWKLHLY ″ B*3501 55 ″ 104 13 ″ ″ 500 510 11 GWKLHLYSHPI 416 B*0801 32 0,99 32 13 ″ ″ 501 510 10 WKLHLYSHPI 417 B*1301 54 ″ 53 13 ″ ″ 501 510 10 WKLHLYSHPI ″ B*1302 27 ″ 27 13 ″ ″ 501 510 10 WKLHLYSHPI ″ B*3701 43 ″ 42 13 ″ ″ 501 510 10 WKLHLYSHPI ″ B*3901 69 ″ 68 13 ″ ″ 501 510 10 WKLHLYSHPI ″ B*5201 78 ″ 78 13 ″ ″ 502 510 9 KLHLYSHPI 418 A*0201 49 ″ 48 13 ″ ″ 502 510 9 KLHLYSHPI ″ A*3201 77 ″ 77 13 ″ ″ 503 510 8 LHLYSHPI 419 B*1402 78 ″ 77 13 ″ ″ 503 510 8 LHLYSHPI ″ B*2702 10 ″ 10 13 ″ ″ 503 510 8 LHLYSHPI ″ B*3801 92 ″ 91 13 ″ ″ 503 510 8 LHLYSHPI ″ B*5101 52 ″ 51 13 ″ ″ 503 510 8 LHLYSHPI ″ B*5201 84 ″ 84 13 ″ ″ 502 511 10 KLHLYSHPIV 420 A*0201 13 0,55 7 13 ″ ″ 502 511 10 KLHLYSHPIV ″ A*3001 98 ″ 54 13 ″ ″ 503 511 9 LHLYSHPIV 421 B*5101 3 ″ 2 13 ″ ″ 504 511 8 HLYSHPIV 422 A*0201 56 ″ 30 13 ″ ″ 504 511 8 HLYSHPIV ″ B*0801 25 ″ 14 13 ″ ″ 502 512 11 KLHLYSHPIVL 423 A*3201 41 1,95 80 13 ″ ″ 502 512 11 KLHLYSHPIVL ″ B*0801 27 ″ 53 13 ″ ″ 502 512 11 KLHLYSHPIVL ″ B*4801 56 ″ 109 13 ″ ″ 503 512 10 LHLYSHPIVL 424 B*1402 91 ″ 177 13 ″ ″ 503 512 10 LHLYSHPIVL ″ B*3801 78 ″ 151 13 ″ ″ 503 512 10 LHLYSHPIVL ″ B*3901 83 ″ 162 13 ″ ″ 504 512 9 HLYSHPIVL 425 A*0201 18 ″ 35 13 ″ ″ 504 512 9 HLYSHPIVL ″ B*1402 83 ″ 162 13 ″ ″ 504 512 9 HLYSHPIVL ″ B*1502 24 ″ 47 13 ″ ″ 504 512 9 HLYSHPIVL ″ B*3901 91 ″ 177 13 ″ ″ 505 512 8 LYSHPIVL 426 A*2301 22 ″ 44 13 ″ ″ 505 512 8 LYSHPIVL ″ A*2402 46 ″ 89 13 ″ ″ 504 514 11 HLYSHPIVLGF 427 A*2501 43 1,62 69 13 ″ ″ 504 514 11 HLYSHPIVLGF ″ A*2601 10 ″ 17 13 ″ ″ 504 514 11 HLYSHPIVLGF ″ A*3201 100 ″ 162 13 ″ ″ 504 514 11 HLYSHPIVLGF ″ B*1402 30 ″ 49 13 ″ ″ 504 514 11 HLYSHPIVLGF ″ B*1501 80 ″ 129 13 ″ ″ 504 514 11 HLYSHPIVLGF ″ B*1502 96 ″ 156 13 ″ ″ 504 514 11 HLYSHPIVLGF ″ B*1525 90 ″ 145 13 ″ ″ 505 514 10 LYSHPIVLGF 428 A*2301 84 ″ 136 13 ″ ″ 505 514 10 LYSHPIVLGF ″ A*2402 86 ″ 139 13 ″ ″ 505 514 10 LYSHPIVLGF ″ A*2902 76 ″ 123 13 ″ ″ 506 514 9 YSHPIVLGF 429 B*4601 64 ″ 103 13 ″ ″ 506 514 9 YSHPIVLGF ″ B*5801 71 ″ 115 13 ″ ″ 506 514 9 YSHPIVLGF ″ B*5802 59 ″ 96 13 ″ ″ Cumulative BCI Class Iscore: 15733 524 531 8 SPFLLAQF 432 B*1402 67 1,59 106 14 524 559 524 531 8 SPFLLAQF ″ B*1502 6 ″ 9 14 ″ ″ 524 531 8 SPFLLAQF ″ B*3503 61 ″ 97 14 ″ ″ 524 531 8 SPFLLAQF ″ B*5301 72 ″ 115 14 ″ ″ 524 532 9 SPFLLAQFT 433 B*5601 17 0,30 5 14 ″ ″ 524 533 10 SPFLLAQFTS 434 A*3201 5 0,76 3 14 ″ ″ 524 533 10 SPFLLAQFTS ″ B*3501 1 ″ 1 14 ″ ″ 524 533 10 SPFLLAQFTS ″ B*5601 27 ″ 21 14 ″ ″ 526 533 8 FLLAQFTS 435 A*0201 42 ″ 32 14 ″ ″ 524 534 11 SPFLLAQFTSA 436 B*0702 46 0,92 43 14 ″ ″ 524 534 11 SPFLLAQFTSA ″ B*3503 3 ″ 2 14 ″ ″ 524 534 11 SPFLLAQFTSA ″ B*5101 25 ″ 23 14 ″ ″ 524 534 11 SPFLLAQFTSA ″ B*5501 98 ″ 90 14 ″ ″ 524 534 11 SPFLLAQFTSA ″ B*5601 95 ″ 88 14 ″ ″ 526 534 9 FLLAQFTSA 437 A*0201 84 ″ 78 14 ″ ″ 526 534 9 FLLAQFTSA ″ A*0206 98 ″ 91 14 ″ ″ 526 534 9 FLLAQFTSA ″ B*0801 78 ″ 72 14 ″ ″ 526 535 10 FLLAQFTSAI 438 A*0201 76 0,94 71 14 ″ ″ 526 535 10 FLLAQFTSAI ″ A*0206 79 ″ 75 14 ″ ″ 526 535 10 FLLAQFTSAI ″ B*1302 11 ″ 11 14 ″ ″ 526 535 10 FLLAQFTSAI ″ B*3801 47 ″ 44 14 ″ ″ 526 535 10 FLLAQFTSAI ″ B*4601 11 ″ 11 14 ″ ″ 526 535 10 FLLAQFTSAI ″ B*5201 14 ″ 13 14 ″ ″ 527 535 9 LLAQFTSAI 439 A*3201 3 ″ 3 14 ″ ″ 527 535 9 LLAQFTSAI ″ B*1525 17 ″ 16 14 ″ ″ 527 535 9 LLAQFTSAI ″ B*5501 19 ″ 18 14 ″ ″ 528 535 8 LAQFTSAI 440 B*5101 62 ″ 58 14 ″ ″ 528 535 8 LAQFTSAI ″ B*5201 76 ″ 72 14 ″ ″ 528 535 8 LAQFTSAI ″ B*5301 5 ″ 5 14 ″ ″ 527 537 11 LLAQFTSAICS 441 A*6802 22 0,41 9 14 ″ ″ 528 538 11 LAQFTSAICSV 442 B*5101 13 1,40 19 14 ″ ″ 528 538 11 LAQFTSAICSV ″ B*5201 12 ″ 16 14 ″ ″ 529 538 10 AQFTsAICSV 443 A*0201 55 ″ 77 14 ″ ″ 529 538 10 AQFTSAICSV ″ A*0206 85 ″ 119 14 ″ ″ 529 538 10 AQFTSAICSV ″ B*1301 83 ″ 116 14 ″ ″ 529 538 10 AQFTSAICSV ″ B*1302 46 ″ 65 14 ″ ″ 529 538 10 AQFTSAICSV ″ B*3701 14 ″ 20 14 ″ ″ 529 538 10 AQFTSAICSV ″ B*3901 10 ″ 15 14 ″ ″ 529 538 10 AQFTSAICSV ″ B*4801 77 ″ 108 14 ″ ″ 529 538 10 AQFTSAICSV ″ B*4901 30 ″ 43 14 ″ ″ 529 538 10 AQFTSAICSV ″ B*5001 64 ″ 90 14 ″ ″ 529 538 10 AQFTSAICSV ″ B*5201 82 ″ 115 14 ″ ″ 531 538 8 FTSAICSV 444 A*2501 82 ″ 114 14 ″ ″ 531 538 8 FTSAICSV ″ A*2601 49 ″ 68 14 ″ ″ 529 539 11 AQFTSAICSVV 445 B*1301 75 1,34 100 14 ″ ″ 529 539 11 AQFTSAICSVV ″ B*1302 41 ″ 55 14 ″ ″ 529 539 11 AQFTSAICSVV ″ B*4002 20 ″ 27 14 ″ ″ 529 539 11 AQFTSAICSVV ″ B*4801 62 ″ 83 14 ″ ″ 529 539 11 AQFTSAICSVV ″ B*4901 26 ″ 35 14 ″ ″ 529 539 11 AQFTSAICSVV ″ B*5001 60 ″ 81 14 ″ ″ 529 539 11 AQFTSAICSVV ″ B*5201 53 ″ 71 14 ″ ″ 531 539 9 FTSAICSVV 446 A*6802 49 ″ 65 14 ″ ″ 531 539 9 FTSAICSVV ″ B*4601 31 ″ 42 14 ″ ″ 531 539 9 FTSAICSVV ″ B*5201 2 ″ 3 14 ″ ″ 531 539 9 FTSAICSVV ″ B*5601 4 ″ 5 14 ″ ″ 530 540 11 QFTSAICSVVR 447 A*3303 30 1,19 35 14 ″ ″ 531 540 10 FTSAICSVVR 448 A*3101 38 ″ 45 14 ″ ″ 531 540 10 FTSAICSVVR ″ A*3303 92 ″ 109 14 ″ ″ 531 540 10 FTSAICSVVR ″ A*6801 100 ″ 119 14 ″ ″ 531 540 10 FTSAICSVVR ″ A*7401 68 ″ 81 14 ″ ″ 531 540 10 FTSAICSVVR ″ B*5701 23 ″ 27 14 ″ ″ 532 540 9 TSAICSVVR 449 A*6801 82 ″ 98 14 ″ ″ 533 540 8 SAICSVVR 450 A*3101 11 ″ 14 14 ″ ″ 533 540 8 SAICSVVR ″ A*3303 39 ″ 47 14 ″ ″ 533 540 8 SAICSVVR ″ A*6801 81 ″ 96 14 ″ ″ 531 541 11 FTSAICSVVRR 451 A*1101 2 1,69 4 14 ″ ″ 531 541 11 FTSAICSVVRR ″ A*3101 32 ″ 54 14 ″ ″ 531 541 11 FTSAICSVVRR ″ A*3303 96 ″ 162 14 ″ ″ 531 541 11 FTSAICSVVRR ″ A*7401 77 ″ 130 14 ″ ″ 532 541 10 TSAICSVVRR 452 A*3101 37 ″ 62 14 ″ ″ 532 541 10 TSAICSVVRR ″ A*6801 99 ″ 167 14 ″ ″ 533 541 9 SAICSVVRR 453 A*3101 6 ″ 11 14 ″ ″ 533 541 9 SAICSVVRR ″ A*3303 63 ″ 107 14 ″ ″ 533 541 9 SAICSVVRR ″ A*6801 85 ″ 144 14 ″ ″ 533 541 9 SAICSVVRR ″ A*7401 46 ″ 78 14 ″ ″ 534 541 8 AICSVVRR 454 A*3101 56 ″ 94 14 ″ ″ 534 541 8 AICSVVRR ″ A*7401 84 ″ 142 14 ″ ″ 533 543 11 SAICSVVRRAF 455 A*2501 10 1,06 11 14 ″ ″ 533 543 11 SAICSVVRRAF ″ B*0702 12 ″ 12 14 ″ ″ 533 543 11 SAICSVVRRAF ″ B*1501 78 ″ 83 14 ″ ″ 533 543 11 SAICSVVRRAF ″ B*1502 94 ″ 100 14 ″ ″ 533 543 11 SAICSVVRRAF ″ B*1525 88 ″ 94 14 ″ ″ 533 543 11 SAICSVVRRAF ″ B*3501 71 ″ 75 14 ″ ″ 533 543 11 SAICSVVRRAF ″ B*3503 31 ″ 33 14 ″ ″ 533 543 11 SAICSVVRRAF ″ B*4601 90 ″ 96 14 ″ ″ 536 543 8 CSVVRRAF 456 B*1502 30 ″ 31 14 ″ ″ 536 543 8 CSVVRRAF ″ B*1525 3 ″ 4 14 ″ ″ 536 543 8 CSVVRRAF ″ B*4601 36 ″ 38 14 ″ ″ 536 545 10 CSVVRRAFPH 457 B*5801 8 0,14 1 14 ″ ″ 538 545 8 VVRRAFPH 458 A*3001 10 ″ 1 14 ″ ″ 537 546 10 SVVRRAFPHC 459 A*3001 28 0,21 6 14 ″ ″ 537 547 11 SVVRRAFPHCL 460 B*0801 71 1,96 140 14 ″ ″ 539 547 9 VRRAFPHCL 461 B*1402 28 ″ 56 14 ″ ″ 539 547 9 VRRAFPHCL ″ B*2702 51 ″ 99 14 ″ ″ 539 547 9 VRRAFPHCL ″ B*2705 3 ″ 6 14 ″ ″ 540 547 8 RRAFPHCL 462 B*1402 47 ″ 93 14 ″ ″ 540 547 8 RRAFPHCL ″ B*2702 96 ″ 189 14 ″ ″ 540 547 8 RRAFPHCL ″ B*2705 93 ″ 182 14 ″ ″ 540 547 8 RRAFPHCL ″ B*3901 9 ″ 18 14 ″ ″ 540 547 8 RRAFPHCL ″ B*4801 6 ″ 11 14 ″ ″ 538 548 11 VVRRAFPHCLA 463 A*3001 86 1,06 91 14 ″ ″ 540 548 9 RRAFPHCLA 464 B*2702 45 ″ 47 14 ″ ″ 540 548 9 RRAFPHCLA ″ B*2705 39 ″ 41 14 ″ ″ 541 548 8 RAFPHCLA 465 A*3001 68 ″ 72 14 ″ ″ 540 549 10 RRAFPHCLAF 466 B*2702 95 1,82 173 14 ″ ″ 540 549 10 RRAFPHCLAF ″ B*2705 91 ″ 165 14 ″ ″ 541 549 9 RAFPHCLAF 467 A*3201 73 ″ 132 14 ″ ″ 541 549 9 RAFPHCLAF ″ B*1301 79 ″ 143 14 ″ ″ 541 549 9 RAFPHCLAF ″ B*1402 66 ″ 119 14 ″ ″ 541 549 9 RAFPHCLAF ″ B*1501 84 ″ 153 14 ″ ″ 541 549 9 RAFPHCLAF ″ B*3501 68 ″ 124 14 ″ ″ 541 549 9 RAFPHCLAF ″ B*4601 97 ″ 176 14 ″ ″ 541 549 9 RAFPHCLAF ″ B*5201 75 ″ 135 14 ″ ″ 541 549 9 RAFPHCLAF ″ B*5701 59 ″ 107 14 ″ ″ 541 549 9 RAFPHCLAF ″ B*5801 81 ″ 148 14 ″ ″ 542 549 8 AFPHCLAF 468 A*2301 71 ″ 128 14 ″ ″ 542 549 8 AFPHCLAF ″ A*2402 70 ″ 128 14 ″ ″ 543 550 8 FPHCLAFS 469 B*3501 67 0,25 17 14 ″ ″ 543 550 8 FPHCLAFS ″ B*5501 17 ″ 4 14 ″ ″ 543 550 8 FPHCLAFS ″ B*5601 56 ″ 14 14 ″ ″ 541 551 11 RAFPHCLAFSY 470 A*0301 77 1,93 149 14 ″ ″ 541 551 11 RAFPHCLAFSY ″ A*3201 94 ″ 182 14 ″ ″ 541 551 11 RAFPHCLAFSY ″ B*1301 66 ″ 128 14 ″ ″ 541 551 11 RAFPHCLAFSY ″ B*1501 91 ″ 175 14 ″ ″ 541 551 11 RAFPHCLAFSY ″ B*1502 93 ″ 179 14 ″ ″ 541 551 11 RAFPHCLAFSY ″ B*1525 95 ″ 183 14 ″ ″ 541 551 11 RAFPHCLAFSY ″ B*5701 89 ″ 173 14 ″ ″ 541 551 11 RAFPHCLAFSY ″ B*5802 86 ″ 165 14 ″ ″ 542 551 10 AFPHCLAFSY 471 A*2902 94 ″ 181 14 ″ ″ 543 551 9 FPHCLAFSY 472 B*3501 97 ″ 188 14 ″ ″ 543 551 9 FPHCLAFSY ″ B*3503 91 ″ 175 14 ″ ″ 543 551 9 FPHCLAFSY ″ B*5301 98 ″ 190 14 ″ ″ 543 551 9 FPHCLAFSY ″ B*5501 83 ″ 160 14 ″ ″ 542 552 11 AFPHCLAFSYM 473 A*2402 4 1,02 4 14 ″ ″ 543 552 10 FPHCLAFSYM 474 B*0702 64 ″ 65 14 ″ ″ 543 552 10 FPHCLAFSYM ″ B*1402 90 ″ 92 14 ″ ″ 543 552 10 FPHCLAFSYM ″ B*3501 96 ″ 98 14 ″ ″ 543 552 10 FPHCLAFSYM ″ B*3503 99 ″ 100 14 ″ ″ 543 552 10 FPHCLAFSYM ″ B*3901 68 ″ 69 14 ″ ″ 543 552 10 FPHCLAFSYM ″ B*5101 98 ″ 100 14 ″ ″ 543 552 10 FPHCLAFSYM ″ B*5301 97 ″ 98 14 ″ ″ 543 552 10 FPHCLAFSYM ″ B*5501 97 ″ 98 14 ″ ″ 543 552 10 FPHCLAFSYM ″ B*5601 87 ″ 89 14 ″ ″ 545 555 11 HCLAFSYMDDV 475 A*0201 73 0,60 44 14 ″ ″ 547 555 9 LAFSYMDDV 476 B*5101 20 ″ 12 14 ″ ″ 547 556 10 LAFSYMDDVV 477 B*5201 51 0,34 17 14 ″ ″ 549 556 8 FSYMDDVV 478 B*4601 34 ″ 12 14 ″ ″ 549 556 8 FSYMDDVV ″ B*5101 23 ″ 8 14 ″ ″ 549 556 8 FSYMDDVV ″ B*5201 39 ″ 13 14 ″ ″ 547 557 11 LAFSYMDDVVL 479 B*3503 11 1,21 13 14 ″ ″ 547 557 11 LAFSYMDDVVL ″ B*3801 29 ″ 35 14 ″ ″ 547 557 11 LAFSYMDDVVL ″ B*3901 19 ″ 24 14 ″ ″ 547 557 11 LAFSYMDDVVL ″ B*4801 23 ″ 28 14 ″ ″ 549 557 9 FSYMDDVVL 480 B*3901 25 ″ 30 14 ″ ″ 549 557 9 FSYMDDVVL ″ B*4601 62 ″ 76 14 ″ ″ 550 557 8 SYMDDVVL 481 A*2301 38 ″ 46 14 ″ ″ 550 557 8 SYMDDVVL ″ A*2402 47 ″ 57 14 ″ ″ 551 559 9 YMDDVVLGA 482 A*0101 66 1,49 98 14 ″ ″ 551 559 9 YMDDVVLGA ″ A*0201 100 ″ 149 14 ″ ″ 551 559 9 YMDDVVLGA ″ A*0206 71 ″ 105 14 ″ ″ 552 559 8 MDDVVLGA 483 A*6802 34 ″ 50 14 ″ ″ Cumulative Class I-BCI score: 12015 526 533 8 FLLAQFTS 435 A*0201 42 0,76 32 15 526 559 524 534 11 SPFLLAQFTSA 436 B*0702 46 0,92 43 15 ″ ″ 524 534 11 SPFLLAQFTSA ″ B*3503 3 ″ 2 15 ″ ″ 524 534 11 SPFLLAQFTSA ″ B*5101 25 ″ 23 15 ″ ″ 524 534 11 SPFLLAQFTSA ″ B*5501 98 ″ 90 15 ″ ″ 524 534 11 SPFLLAQFTSA ″ B*5601 95 ″ 88 15 ″ ″ 526 534 9 FLLAQFTSA 437 A*0201 84 ″ 78 15 ″ ″ 526 534 9 FLLAQFTSA ″ A*0206 98 ″ 91 15 ″ ″ 526 534 9 FLLAQFTSA ″ B*0801 78 ″ 72 15 ″ ″ 526 535 10 FLLAQFTSAI 438 A*0201 76 0,94 71 15 ″ ″ 526 535 10 FLLAQFTSAI ″ A*0206 79 ″ 75 15 ″ ″ 526 535 10 FLLAQFTSAI ″ B*1302 11 ″ 11 15 ″ ″ 526 535 10 FLLAQFTSAI ″ B*3801 47 ″ 44 15 ″ ″ 526 535 10 FLLAQFTSAI ″ B*4601 11 ″ 11 15 ″ ″ 526 535 10 FLLAQFTSAI ″ B*5201 14 ″ 13 15 ″ ″ 527 535 9 LLAQFTSAI 439 A*3201 3 ″ 3 15 ″ ″ 527 535 9 LLAQFTSAI ″ B*1525 17 ″ 16 15 ″ ″ 527 535 9 LLAQFTSAI ″ B*5501 19 ″ 18 15 ″ ″ 528 535 8 LAQFTSAI 440 B*5101 62 ″ 58 15 ″ ″ 528 535 8 LAQFTSAI ″ B*5201 76 ″ 72 15 ″ ″ 528 535 8 LAQFTSAI ″ B*5301 5 ″ 5 15 ″ ″ 527 537 11 LLAQFTSAICS 441 A*6802 22 0,41 9 15 ″ ″ 528 538 11 LAQFTSAICSV 442 B*5101 13 1,40 19 15 ″ ″ 528 538 11 LAQFTSAICSV ″ B*5201 12 ″ 16 15 ″ ″ 529 538 10 AQFTsAICSV 443 A*0201 55 ″ 77 15 ″ ″ 529 538 10 AQFTSAICSV ″ A*0206 85 ″ 119 15 ″ ″ 529 538 10 AQFTSAICSV ″ B*1301 83 ″ 116 15 ″ ″ 529 538 10 AQFTSAICSV ″ B*1302 46 ″ 65 15 ″ ″ 529 538 10 AQFTSAICSV ″ B*3701 14 ″ 20 15 ″ ″ 529 538 10 AQFTSAICSV ″ B*3901 10 ″ 15 15 ″ ″ 529 538 10 AQFTSAICSV ″ B*4801 77 ″ 108 15 ″ ″ 529 538 10 AQFTSAICSV ″ B*4901 30 ″ 43 15 ″ ″ 529 538 10 AQFTSAICSV ″ B*5001 64 ″ 90 15 ″ ″ 529 538 10 AQFTSAICSV ″ B*5201 82 ″ 115 15 ″ ″ 531 538 8 FTSAICSV 444 A*2501 82 ″ 114 15 ″ ″ 531 538 8 FTSAICSV ″ A*2601 49 ″ 68 15 ″ ″ 529 539 11 AQFTSAICSVV 445 B*1301 75 1,34 100 15 ″ ″ 529 539 11 AQFTSAICSVV ″ B*1302 41 ″ 55 15 ″ ″ 529 539 11 AQFTSAICSVV ″ B*4002 20 ″ 27 15 ″ ″ 529 539 11 AQFTSAICSVV ″ B*4801 62 ″ 83 15 ″ ″ 529 539 11 AQFTSAICSVV ″ B*4901 26 ″ 35 15 ″ ″ 529 539 11 AQFTSAICSVV ″ B*5001 60 ″ 81 15 ″ ″ 529 539 11 AQFTSAICSVV ″ B*5201 53 ″ 71 15 ″ ″ 531 539 9 FTSAICSVV 446 A*6802 49 ″ 65 15 ″ ″ 531 539 9 FTSAICSVV ″ B*4601 31 ″ 42 15 ″ ″ 531 539 9 FTSAICSVV ″ B*5201 2 ″ 3 15 ″ ″ 531 539 9 FTSAICSVV ″ B*5601 4 ″ 5 15 ″ ″ 530 540 11 QFTSAICSVVR 447 A*3303 30 1,19 35 15 ″ ″ 531 540 10 FTSAICSVVR 448 A*3101 38 ″ 45 15 ″ ″ 531 540 10 FTSAICSVVR ″ A*3303 92 ″ 109 15 ″ ″ 531 540 10 FTSAICSVVR ″ A*6801 100 ″ 119 15 ″ ″ 531 540 10 FTSAICSVVR ″ A*7401 68 ″ 81 15 ″ ″ 531 540 10 FTSAICSVVR ″ B*5701 23 ″ 27 15 ″ ″ 532 540 9 TSAICSVVR 449 A*6801 82 ″ 98 15 ″ ″ 533 540 8 SAICSVVR 450 A*3101 11 ″ 14 15 ″ ″ 533 540 8 SAICSVVR ″ A*3303 39 ″ 47 15 ″ ″ 533 540 8 SAICSVVR ″ A*6801 81 ″ 96 15 ″ ″ 531 541 11 FTSAICSVVRR 451 A*1101 2 1,69 4 15 ″ ″ 531 541 11 FTSAICSVVRR ″ A*3101 32 ″ 54 15 ″ ″ 531 541 11 FTSAICSVVRR ″ A*3303 96 ″ 162 15 ″ ″ 531 541 11 FTSAICSVVRR ″ A*7401 77 ″ 130 15 ″ ″ 532 541 10 TSAICSVVRR 452 A*3101 37 ″ 62 15 ″ ″ 532 541 10 TSAICSVVRR ″ A*6801 99 ″ 167 15 ″ ″ 533 541 9 SAICSVVRR 453 A*3101 6 ″ 11 15 ″ ″ 533 541 9 SAICSVVRR ″ A*3303 63 ″ 107 15 ″ ″ 533 541 9 SAICSVVRR ″ A*6801 85 ″ 144 15 ″ ″ 533 541 9 SAICSVVRR ″ A*7401 46 ″ 78 15 ″ ″ 534 541 8 AICSVVRR 454 A*3101 56 ″ 94 15 ″ ″ 534 541 8 AICSVVRR ″ A*7401 84 ″ 142 15 ″ ″ 533 543 11 SAICSVVRRAF 455 A*2501 10 1,06 11 15 ″ ″ 533 543 11 SAICSVVRRAF ″ B*0702 12 ″ 12 15 ″ ″ 533 543 11 SAICSVVRRAF ″ B*1501 78 ″ 83 15 ″ ″ 533 543 11 SAICSVVRRAF ″ B*1502 94 ″ 100 15 ″ ″ 533 543 11 SAICSVVRRAF ″ B*1525 88 ″ 94 15 ″ ″ 533 543 11 SAICSVVRRAF ″ B*3501 71 ″ 75 15 ″ ″ 533 543 11 SAICSVVRRAF ″ B*3503 31 ″ 33 15 ″ ″ 533 543 11 SAICSVVRRAF ″ B*4601 90 ″ 96 15 ″ ″ 536 543 8 CSVVRRAF 456 B*1502 30 ″ 31 15 ″ ″ 536 543 8 CSVVRRAF ″ B*1525 3 ″ 4 15 ″ ″ 536 543 8 CSVVRRAF ″ B*4601 36 ″ 38 15 ″ ″ 536 545 10 CSVVRRAFPH 457 B*5801 8 0,14 1 15 ″ ″ 538 545 8 VVRRAFPH 458 A*3001 10 ″ 1 15 ″ ″ 537 546 10 SVVRRAFPHC 459 A*3001 28 0,21 6 15 ″ ″ 537 547 11 SVVRRAFPHCL 460 B*0801 71 1,96 140 15 ″ ″ 539 547 9 VRRAFPHCL 461 B*1402 28 ″ 56 15 ″ ″ 539 547 9 VRRAFPHCL ″ B*2702 51 ″ 99 15 ″ ″ 539 547 9 VRRAFPHCL ″ B*2705 3 ″ 6 15 ″ ″ 540 547 8 RRAFPHCL 462 B*1402 47 ″ 93 15 ″ ″ 540 547 8 RRAFPHCL ″ B*2702 96 ″ 189 15 ″ ″ 540 547 8 RRAFPHCL ″ B*2705 93 ″ 182 15 ″ ″ 540 547 8 RRAFPHCL ″ B*3901 9 ″ 18 15 ″ ″ 540 547 8 RRAFPHCL ″ B*4801 6 ″ 11 15 ″ ″ 538 548 11 VVRRAFPHCLA 463 A*3001 86 1,06 91 15 ″ ″ 540 548 9 RRAFPHCLA 464 B*2702 45 ″ 47 15 ″ ″ 540 548 9 RRAFPHCLA ″ B*2705 39 ″ 41 15 ″ ″ 541 548 8 RAFPHCLA 465 A*3001 68 ″ 72 15 ″ ″ 540 549 10 RRAFPHCLAF 466 B*2702 95 1,82 173 15 ″ ″ 540 549 10 RRAFPHCLAF ″ B*2705 91 ″ 165 15 ″ ″ 541 549 9 RAFPHCLAF 467 A*3201 73 ″ 132 15 ″ ″ 541 549 9 RAFPHCLAF ″ B*1301 79 ″ 143 15 ″ ″ 541 549 9 RAFPHCLAF ″ B*1402 66 ″ 119 15 ″ ″ 541 549 9 RAFPHCLAF ″ B*1501 84 ″ 153 15 ″ ″ 541 549 9 RAFPHCLAF ″ B*3501 68 ″ 124 15 ″ ″ 541 549 9 RAFPHCLAF ″ B*4601 97 ″ 176 15 ″ ″ 541 549 9 RAFPHCLAF ″ B*5201 75 ″ 135 15 ″ ″ 541 549 9 RAFPHCLAF ″ B*5701 59 ″ 107 15 ″ ″ 541 549 9 RAFPHCLAF ″ B*5801 81 ″ 148 15 ″ ″ 542 549 8 AFPHCLAF 468 A*2301 71 ″ 128 15 ″ ″ 542 549 8 AFPHCLAF ″ A*2402 70 ″ 128 15 ″ ″ 543 550 8 FPHCLAFS 469 B*3501 67 0,25 17 15 ″ ″ 543 550 8 FPHCLAFS ″ B*5501 17 ″ 4 15 ″ ″ 543 550 8 FPHCLAFS ″ B*5601 56 ″ 14 15 ″ ″ 541 551 11 RAFPHCLAFSY 470 A*0301 77 1,93 149 15 ″ ″ 541 551 11 RAFPHCLAFSY ″ A*3201 94 ″ 182 15 ″ ″ 541 551 11 RAFPHCLAFSY ″ B*1301 66 ″ 128 15 ″ ″ 541 551 11 RAFPHCLAFSY ″ B*1501 91 ″ 175 15 ″ ″ 541 551 11 RAFPHCLAFSY ″ B*1502 93 ″ 179 15 ″ ″ 541 551 11 RAFPHCLAFSY ″ B*1525 95 ″ 183 15 ″ ″ 541 551 11 RAFPHCLAFSY ″ B*5701 89 ″ 173 15 ″ ″ 541 551 11 RAFPHCLAFSY ″ B*5802 86 ″ 165 15 ″ ″ 542 551 10 AFPHCLAFSY 471 A*2902 94 ″ 181 15 ″ ″ 543 551 9 FPHCLAFSY 472 B*3501 97 ″ 188 15 ″ ″ 543 551 9 FPHCLAFSY ″ B*3503 91 ″ 175 15 ″ ″ 543 551 9 FPHCLAFSY ″ B*5301 98 ″ 190 15 ″ ″ 543 551 9 FPHCLAFSY ″ B*5501 83 ″ 160 15 ″ ″ 542 552 11 AFPHCLAFSYM 473 A*2402 4 1,02 4 15 ″ ″ 543 552 10 FPHCLAFSYM 474 B*0702 64 ″ 65 15 ″ ″ 543 552 10 FPHCLAFSYM ″ B*1402 90 ″ 92 15 ″ ″ 543 552 10 FPHCLAFSYM ″ B*3501 96 ″ 98 15 ″ ″ 543 552 10 FPHCLAFSYM ″ B*3503 99 ″ 100 15 ″ ″ 543 552 10 FPHCLAFSYM ″ B*3901 68 ″ 69 15 ″ ″ 543 552 10 FPHCLAFSYM ″ B*5101 98 ″ 100 15 ″ ″ 543 552 10 FPHCLAFSYM ″ B*5301 97 ″ 98 15 ″ ″ 543 552 10 FPHCLAFSYM ″ B*5501 97 ″ 98 15 ″ ″ 543 552 10 FPHCLAFSYM ″ B*5601 87 ″ 89 15 ″ ″ 545 555 11 HCLAFSYMDDV 475 A*0201 73 0,60 44 15 ″ ″ 547 555 9 LAFSYMDDV 476 B*5101 20 ″ 12 15 ″ ″ 547 556 10 LAFSYMDDVV 477 B*5201 51 0,34 17 15 ″ ″ 549 556 8 FSYMDDVV 478 B*4601 34 ″ 12 15 ″ ″ 549 556 8 FSYMDDVV ″ B*5101 23 ″ 8 15 ″ ″ 549 556 8 FSYMDDVV ″ B*5201 39 ″ 13 15 ″ ″ 547 557 11 LAFSYMDDVVL 479 B*3503 11 1,21 13 15 ″ ″ 547 557 11 LAFSYMDDVVL ″ B*3801 29 ″ 35 15 ″ ″ 547 557 11 LAFSYMDDVVL ″ B*3901 19 ″ 24 15 ″ ″ 547 557 11 LAFSYMDDVVL ″ B*4801 23 ″ 28 15 ″ ″ 549 557 9 FSYMDDVVL 480 B*3901 25 ″ 30 15 ″ ″ 549 557 9 FSYMDDVVL ″ B*4601 62 ″ 76 15 ″ ″ 550 557 8 SYMDDVVL 481 A*2301 38 ″ 46 15 ″ ″ 550 557 8 SYMDDVVL ″ A*2402 47 ″ 57 15 ″ ″ 551 559 9 YMDDVVLGA 482 A*0101 66 1,49 98 15 ″ ″ 551 559 9 YMDDVVLGA ″ A*0201 100 ″ 149 15 ″ ″ 551 559 9 YMDDVVLGA ″ A*0206 71 ″ 105 15 ″ ″ 552 559 8 MDDVVLGA 483 A*6802 34 ″ 50 15 ″ ″ Cumulative Class I-BCI score: 11658 565 572 8 RESLYTAV 486 B*1301 93 1,67 155 16 565 598 565 572 8 RESLYTAV ″ B*1302 31 ″ 52 16 ″ ″ 565 572 8 RESLYTAV ″ B*3701 81 ″ 135 16 ″ ″ 565 572 8 RESLYTAV ″ B*4001 91 ″ 153 16 ″ ″ 565 572 8 RESLYTAV ″ B*4002 90 ″ 151 16 ″ ″ 565 572 8 RESLYTAV ″ B*4402 65 ″ 109 16 ″ ″ 565 572 8 RESLYTAV ″ B*4403 52 ″ 87 16 ″ ″ 565 572 8 RESLYTAV ″ B*4801 44 ″ 74 16 ″ ″ 565 572 8 RESLYTAV ″ B*4901 87 ″ 145 16 ″ ″ 565 572 8 RESLYTAV ″ B*5001 88 ″ 147 16 ″ ″ 565 573 9 RESLYTAVT 487 B*4002 40 1,11 45 16 ″ ″ 565 573 9 RESLYTAVT ″ B*5001 56 ″ 62 16 ″ ″ 565 574 10 RESLYTAVTN 488 B*4002 35 0,69 24 16 ″ ″ 565 575 11 RESLYTAVTNF 489 B*1301 73 1,85 136 16 ″ ″ 565 575 11 RESLYTAVTNF ″ B*1801 81 ″ 150 16 ″ ″ 565 575 11 RESLYTAVTNF ″ B*4001 78 ″ 145 16 ″ ″ 565 575 11 RESLYTAVTNF ″ B*4002 75 ″ 139 16 ″ ″ 565 575 11 RESLYTAVTNF ″ B*4402 96 ″ 178 16 ″ ″ 565 575 11 RESLYTAVTNF ″ B*4403 92 ″ 170 16 ″ ″ 565 575 11 RESLYTAVTNF ″ B*4901 70 ″ 129 16 ″ ″ 565 575 11 RESLYTAVTNF ″ B*5001 68 ″ 126 16 ″ ″ 566 575 10 ESLYTAVTNF 490 A*2601 95 ″ 176 16 ″ ″ 567 575 9 SLYTAVTNF 491 B*1501 64 ″ 119 16 ″ ″ 567 575 9 SLYTAVTNF ″ B*1525 86 ″ 160 16 ″ ″ 568 575 8 LYTAVTNF 492 A*2301 90 ″ 166 16 ″ ″ 568 575 8 LYTAVTNF ″ A*2402 91 ″ 169 16 ″ ″ 567 576 10 SLYTAVTNFL 493 A*0201 64 1,69 109 16 ″ ″ 568 576 9 LYTAVTNFL 494 A*2301 16 ″ 26 16 ″ ″ 568 576 9 LYTAVTNFL ″ A*2402 53 ″ 89 16 ″ ″ 569 576 8 YTAVTNFL 495 A*0101 2 ″ 3 16 ″ ″ 569 576 8 YTAVTNFL ″ A*2501 71 ″ 121 16 ″ ″ 569 576 8 YTAVTNFL ″ A*2601 59 ″ 100 16 ″ ″ 569 576 8 YTAVTNFL ″ B*4601 80 ″ 136 16 ″ ″ 567 577 11 SLYTAVTNFLL 496 A*3201 48 1,86 90 16 ″ ″ 568 577 10 LYTAVTNFLL 497 A*2301 60 ″ 112 16 ″ ″ 568 577 10 LYTAVTNFLL ″ A*2402 67 ″ 124 16 ″ ″ 568 577 10 LYTAVTNFLL ″ B*3801 8 ″ 15 16 ″ ″ 569 577 9 YTAVTNFLL 498 A*0101 70 ″ 130 16 ″ ″ 569 577 9 YTAVTNFLL ″ A*6802 28 ″ 52 16 ″ ″ 569 577 9 YTAVTNFLL ″ B*5801 41 ″ 75 16 ″ ″ 569 579 11 YTAVTNFLLSL 499 A*0101 58 1,91 112 16 ″ ″ 569 579 11 YTAVTNFLLSL ″ A*2501 69 ″ 132 16 ″ ″ 569 579 11 YTAVTNFLLSL ″ A*2601 56 ″ 108 16 ″ ″ 569 579 11 YTAVTNFLLSL ″ B*3801 43 ″ 82 16 ″ ″ 569 579 11 YTAVTNFLLSL ″ B*4601 89 ″ 169 16 ″ ″ 569 579 11 YTAVTNFLLSL ″ B*5801 14 ″ 26 16 ″ ″ 572 579 8 VTNFLLSL 500 A*3201 26 ″ 49 16 ″ ″ 572 579 8 VTNFLLSL ″ B*0702 23 ″ 44 16 ″ ″ 571 581 11 AVTNFLLSLGI 501 A*3201 9 1,49 14 16 ″ ″ 573 581 9 TNFLLSLGI 502 B*5201 31 ″ 47 16 ″ ″ 575 583 9 FLLSLGIHL 503 A*0201 82 1,27 104 16 ″ ″ 575 583 9 FLLSLGIHL ″ A*0206 46 ″ 58 16 ″ ″ 576 583 8 LLSLGIHL 504 B*0702 90 ″ 114 16 ″ ″ 578 585 8 SLGIHLNP 505 A*0201 98 0,14 14 16 ″ ″ 576 586 11 LLSLGIHLNPN 506 A*0206 75 0,09 7 16 ″ ″ 577 587 11 LSLGIHLNPNK 507 A*0301 10 0,12 1 16 ″ ″ 577 587 11 LSLGIHLNPNK ″ A*1101 50 ″ 6 16 ″ ″ 578 587 10 SLGIHLNPNK 508 A*0301 30 ″ 3 16 ″ ″ 578 587 10 SLGIHLNPNK ″ A*1101 24 ″ 3 16 ″ ″ 580 587 8 GIHLNPNK 509 A*0301 26 ″ 3 16 ″ ″ 580 587 8 GIHLNPNK ″ A*1101 17 ″ 2 16 ″ ″ 582 589 8 HLNPNKTK 510 A*0301 51 1,61 82 16 ″ ″ 582 590 9 HLNPNKTKR 511 A*3101 85 1,52 129 16 ″ ″ 582 590 9 HLNPNKTKR ″ A*3303 54 ″ 81 16 ″ ″ 582 590 9 HLNPNKTKR ″ A*7401 20 ″ 30 16 ″ ″ 584 591 8 NPNKTKRW 512 B*5301 46 1,80 83 16 ″ ″ 585 594 10 PNKTKRWGYS 513 A*3201 55 0,53 29 16 ″ ″ 587 594 8 KTKRWGYS 514 A*3001 67 ″ 36 16 ″ ″ 586 595 10 NKTKRWGYSL 515 B*1402 46 1,81 84 16 ″ ″ 587 595 9 KTKRWGYSL 516 A*3001 64 ″ 116 16 ″ ″ 587 595 9 KTKRWGYSL ″ A*3201 85 ″ 154 16 ″ ″ 587 595 9 KTKRWGYSL ″ B*5701 50 ″ 91 16 ″ ″ 587 595 9 KTKRWGYSL ″ B*5802 52 ″ 94 16 ″ ″ 588 595 8 TKRWGYSL 517 B*1402 56 ″ 101 16 ″ ″ 589 596 8 KRWGYSLN 518 B*2702 42 0,19 8 16 ″ ″ 589 596 8 KRWGYSLN ″ B*2705 75 ″ 14 16 ″ ″ 587 597 11 KTKRWGYSLNF 519 A*2402 2 1,95 3 16 ″ ″ 587 597 11 KTKRWGYSLNF ″ A*3001 41 ″ 80 16 ″ ″ 587 597 11 KTKRWGYSLNF ″ A*3002 41 ″ 80 16 ″ ″ 587 597 11 KTKRWGYSLNF ″ A*3201 91 ″ 177 16 ″ ″ 587 597 11 KTKRWGYSLNF ″ B*5701 77 ″ 150 16 ″ ″ 587 597 11 KTKRWGYSLNF ″ B*5801 44 ″ 86 16 ″ ″ 587 597 11 KTKRWGYSLNF ″ B*5802 81 ″ 158 16 ″ ″ 589 597 9 KRWGYSLNF 520 A*3201 12 ″ 24 16 ″ ″ 589 597 9 KRWGYSLNF ″ B*2705 96 ″ 186 16 ″ ″ 590 597 8 RWGYSLNF 521 A*2301 88 ″ 171 16 ″ ″ 590 597 8 RWGYSLNF ″ A*2402 89 ″ 174 16 ″ ″ 590 597 8 RWGYSLNF ″ B*2705 63 ″ 122 16 ″ ″ 589 598 10 KRWGYSLNFM 522 B*2702 100 0,84 84 16 ″ ″ 589 598 10 KRWGYSLNFM ″ B*2705 43 ″ 36 16 ″ ″ 589 598 10 KRWGYSLNFM ″ B*3901 5 ″ 4 16 ″ ″ 590 598 9 RWGYSLNFM 523 A*2402 7 ″ 6 16 ″ ″ Cumulative Class I-BCI score: 8255 585 594 10 PNKTKRWGYS 513 A*3201 55 0,53 29 17 584 617 587 594 8 KTKRWGYS 514 A*3001 67 ″ 36 17 ″ ″ 586 595 10 NKTKRWGYSL 515 B*1402 46 1,81 84 17 ″ ″ 587 595 9 KTKRWGYSL 516 A*3001 64 ″ 116 17 ″ ″ 587 595 9 KTKRWGYSL ″ A*3201 85 ″ 154 17 ″ ″ 587 595 9 KTKRWGYSL ″ B*5701 50 ″ 91 17 ″ ″ 587 595 9 KTKRWGYSL ″ B*5802 52 ″ 94 17 ″ ″ 588 595 8 TKRWGYSL 517 B*1402 56 ″ 101 17 ″ ″ 589 596 8 KRWGYSLN 518 B*2702 42 0,19 8 17 ″ ″ 589 596 8 KRWGYSLN ″ B*2705 75 ″ 14 17 ″ ″ 587 597 11 KTKRWGYSLNF 519 A*2402 2 1,95 3 17 ″ ″ 587 597 11 KTKRWGYSLNF ″ A*3001 41 ″ 80 17 ″ ″ 587 597 11 KTKRWGYSLNF ″ A*3002 41 ″ 80 17 ″ ″ 587 597 11 KTKRWGYSLNF ″ A*3201 91 ″ 177 17 ″ ″ 587 597 11 KTKRWGYSLNF ″ B*5701 77 ″ 150 17 ″ ″ 587 597 11 KTKRWGYSLNF ″ B*5801 44 ″ 86 17 ″ ″ 587 597 11 KTKRWGYSLNF ″ B*5802 81 ″ 158 17 ″ ″ 589 597 9 KRWGYSLNF 520 A*3201 12 ″ 24 17 ″ ″ 589 597 9 KRWGYSLNF ″ B*2705 96 ″ 186 17 ″ ″ 590 597 8 RWGYSLNF 521 A*2301 88 ″ 171 17 ″ ″ 590 597 8 RWGYSLNF ″ A*2402 89 ″ 174 17 ″ ″ 590 597 8 RWGYSLNF ″ B*2705 63 ″ 122 17 ″ ″ 589 598 10 KRWGYSLNFM 522 B*2702 100 0,84 84 17 ″ ″ 589 598 10 KRWGYSLNFM ″ B*2705 43 ″ 36 17 ″ ″ 589 598 10 KRWGYSLNFM ″ B*3901 5 ″ 4 17 ″ ″ 590 598 9 RWGYSLNFM 523 A*2402 7 ″ 6 17 ″ ″ 589 599 11 KRWGYSLNFMG 524 B*2702 57 0,64 36 17 ″ ″ 589 599 11 KRWGYSLNFMG ″ B*2705 24 ″ 15 17 ″ ″ 590 600 11 RWGYSLNFMGY 525 A*3002 82 1,89 155 17 ″ ″ 592 600 9 GYSLNFMGY 526 A*2902 73 ″ 138 17 ″ ″ 593 600 8 YSLNFMGY 527 A*0101 87 ″ 164 17 ″ ″ 593 600 8 YSLNFMGY ″ A*2501 88 ″ 166 17 ″ ″ 593 600 8 YSLNFMGY ″ A*2601 87 ″ 165 17 ″ ″ 593 600 8 YSLNFMGY ″ A*2902 100 ″ 189 17 ″ ″ 593 600 8 YSLNFMGY ″ A*3002 86 ″ 163 17 ″ ″ 593 600 8 YSLNFMGY ″ B*1501 42 ″ 80 17 ″ ″ 593 600 8 YSLNFMGY ″ B*1502 48 ″ 91 17 ″ ″ 593 600 8 YSLNFMGY ″ B*1525 37 ″ 71 17 ″ ″ 593 600 8 YSLNFMGY ″ B*4601 79 ″ 149 17 ″ ″ 593 600 8 YSLNFMGY ″ B*5801 27 ″ 51 17 ″ ″ 593 600 8 YSLNFMGY ″ B*5802 25 ″ 47 17 ″ ″ 591 601 11 WGYSLNFMGYI 528 B*1302 25 0,91 23 17 ″ ″ 591 601 11 WGYSLNFMGYI ″ B*5201 67 ″ 60 17 ″ ″ 593 601 9 YSLNFMGYI 529 A*2501 76 ″ 68 17 ″ ″ 593 601 9 YSLNFMGYI ″ B*4601 30 ″ 27 17 ″ ″ 593 601 9 YSLNFMGYI ″ B*5201 49 ″ 44 17 ″ ″ 593 601 9 YSLNFMGYI ″ B*5802 78 ″ 71 17 ″ ″ 594 601 8 SLNFMGYI 530 A*3201 39 ″ 36 17 ″ ″ 592 602 11 GYSLNFMGYII 531 A*2301 62 0,67 42 17 ″ ″ 592 602 11 GYSLNFMGYII ″ A*2402 68 ″ 46 17 ″ ″ 593 602 10 YSLNFMGYII 532 A*0206 52 ″ 35 17 ″ ″ 593 602 10 YSLNFMGYII ″ B*1301 62 ″ 42 17 ″ ″ 593 602 10 YSLNFMGYII ″ B*1302 39 ″ 27 17 ″ ″ 593 602 10 YSLNFMGYII ″ B*3801 20 ″ 14 17 ″ ″ 593 602 10 YSLNFMGYII ″ B*5201 92 ″ 62 17 ″ ″ 593 602 10 YSLNFMGYII ″ B*5802 4 ″ 3 17 ″ ″ 594 602 9 SLNFMGYII 533 A*3201 71 ″ 48 17 ″ ″ 595 602 8 LNFMGYII 534 B*1302 30 ″ 20 17 ″ ″ 595 602 8 LNFMGYII ″ B*5101 7 ″ 4 17 ″ ″ 595 602 8 LNFMGYII ″ B*5201 90 ″ 61 17 ″ ″ 597 604 8 FMGYIIGS 535 A*0201 36 0,52 19 17 ″ ″ 595 605 11 LNFMGYIIGSW 536 B*5701 5 1,77 8 17 ″ ″ 596 605 10 NFMGYIIGSW 537 A*2301 50 ″ 88 17 ″ ″ 596 605 10 NFMGYIIGSW ″ B*4402 50 ″ 88 17 ″ ″ 597 605 9 FMGYIIGSW 538 B*4601 52 ″ 93 17 ″ ″ 598 605 8 MGYIIGSW 539 A*6802 25 ″ 44 17 ″ ″ 598 605 8 MGYIIGSW ″ B*5201 29 ″ 52 17 ″ ″ 598 605 8 MGYIIGSW ″ B*5301 56 ″ 99 17 ″ ″ 598 605 8 MGYIIGSW ″ B*5701 85 ″ 150 17 ″ ″ 598 605 8 MGYIIGSW ″ B*5801 78 ″ 138 17 ″ ″ 598 605 8 MGYIIGSW ″ B*5802 80 ″ 141 17 ″ ″ 598 608 11 MGYIIGSWGTL 540 B*1402 33 1,71 57 17 ″ ″ 599 608 10 GYIIGSWGTL 541 A*3201 83 ″ 142 17 ″ ″ 600 608 9 YIIGSWGTL 542 A*0206 2 ″ 4 17 ″ ″ 600 608 9 YIIGSWGTL ″ A*2501 92 ″ 157 17 ″ ″ 600 608 9 YIIGSWGTL ″ A*2601 28 ″ 48 17 ″ ″ 600 608 9 YIIGSWGTL ″ B*1502 67 ″ 114 17 ″ ″ 607 614 8 TLPQDHIV 543 A*0201 4 0,56 2 17 ″ ″ 606 616 11 GTLPQDHIVQK 544 A*0301 8 1,05 9 17 ″ ″ 606 616 11 GTLPQDHIVQK ″ A*1101 63 ″ 66 17 ″ ″ 608 617 10 LPQDHIVQKI 545 B*5101 82 1,83 150 17 ″ ″ 608 617 10 LPQDHIVQKI ″ B*5301 26 ″ 48 17 ″ ″ Cumulative BCI Class Iscore: 6396 653 660 8 YPALMPLY 548 A*0101 36 1,81 65 18 653 691 653 660 8 YPALMPLY ″ A*2601 21 ″ 37 18 ″ ″ 653 660 8 YPALMPLY ″ A*2902 41 ″ 75 18 ″ ″ 653 660 8 YPALMPLY ″ B*3501 95 ″ 171 18 ″ ″ 653 660 8 YPALMPLY ″ B*3503 84 ″ 151 18 ″ ″ 653 660 8 YPALMPLY ″ B*5101 38 ″ 69 18 ″ ″ 653 660 8 YPALMPLY ″ B*5301 89 ″ 160 18 ″ ″ 653 660 8 YPALMPLY ″ B*5501 28 ″ 50 18 ″ ″ 653 660 8 YPALMPLY ″ B*5601 37 ″ 67 18 ″ ″ 652 661 10 GYPALMPLYA 549 A*2402 40 1,43 58 18 ″ ″ 653 661 9 YPALMPLYA 550 B*0702 9 ″ 12 18 ″ ″ 653 661 9 YPALMPLYA ″ B*3503 59 ″ 85 18 ″ ″ 653 661 9 YPALMPLYA ″ B*5101 27 ″ 38 18 ″ ″ 653 661 9 YPALMPLYA ″ B*5501 94 ″ 135 18 ″ ″ 653 661 9 YPALMPLYA ″ B*5601 100 ″ 143 18 ″ ″ 653 662 10 YPALMPLYAC 551 B*0702 4 0,21 1 18 ″ ″ 653 662 10 YPALMPLYAC ″ B*3501 72 ″ 15 18 ″ ″ 653 662 10 YPALMPLYAC ″ B*3503 69 ″ 14 18 ″ ″ 653 662 10 YPALMPLYAC ″ B*5301 54 ″ 11 18 ″ ″ 653 662 10 YPALMPLYAC ″ B*5501 70 ″ 15 18 ″ ″ 653 662 10 YPALMPLYAC ″ B*5601 86 ″ 18 18 ″ ″ 655 662 8 ALMPLYAC 552 A*0201 11 ″ 2 18 ″ ″ 653 663 11 YPALMPLYACI 553 B*0702 54 1,19 64 18 ″ ″ 653 663 11 YPALMPLYACI ″ B*1402 40 ″ 48 18 ″ ″ 653 663 11 YPALMPLYACI ″ B*3501 33 ″ 40 18 ″ ″ 653 663 11 YPALMPLYACI ″ B*3503 82 ″ 98 18 ″ ″ 653 663 11 YPALMPLYACI ″ B*5101 100 ″ 119 18 ″ ″ 653 663 11 YPALMPLYACI ″ B*5201 27 ″ 33 18 ″ ″ 653 663 11 YPALMPLYACI ″ B*5301 87 ″ 104 18 ″ ″ 653 663 11 YPALMPLYACI ″ B*5501 69 ″ 82 18 ″ ″ 653 663 11 YPALMPLYACI ″ B*5601 77 ″ 92 18 ″ ″ 655 663 9 ALMPLYACI 554 A*0201 67 ″ 80 18 ″ ″ 657 664 8 MPLYACIQ 555 B*5501 12 0,20 2 18 ″ ″ 657 664 8 MPLYACIQ ″ B*5601 8 ″ 2 18 ″ ″ 657 665 9 MPLYACIQA 556 B*3501 44 1,41 62 18 ″ ″ 657 665 9 MPLYACIQA ″ B*3503 49 ″ 68 18 ″ ″ 657 665 9 MPLYACIQA ″ B*5101 80 ″ 112 18 ″ ″ 657 665 9 MPLYACIQA ″ B*5501 93 ″ 131 18 ″ ″ 657 665 9 MPLYACIQA ″ B*5601 99 ″ 139 18 ″ ″ 657 666 10 MPLYACIQAK 557 B*3501 43 1,01 43 18 ″ ″ 657 666 10 MPLYACIQAK ″ B*5601 3 ″ 3 18 ″ ″ 658 666 9 PLYACIQAK 558 A*0301 74 ″ 75 18 ″ ″ 659 669 11 LYACIQAKQAF 559 A*2301 86 1,07 92 18 ″ ″ 659 669 11 LYACIQAKQAF ″ A*2402 88 ″ 94 18 ″ ″ 660 669 10 YACIQAKQAF 560 B*1502 26 ″ 28 18 ″ ″ 663 671 9 IQAKQAFTF 561 A*2402 84 1,58 133 18 ″ ″ 663 671 9 IQAKQAFTF ″ B*1301 61 ″ 96 18 ″ ″ 663 671 9 IQAKQAFTF ″ B*1501 63 ″ 99 18 ″ ″ 663 671 9 IQAKQAFTF ″ B*1525 71 ″ 112 18 ″ ″ 664 671 8 QAKQAFTF 562 B*1501 8 ″ 12 18 ″ ″ 664 671 8 QAKQAFTF ″ B*1502 37 ″ 59 18 ″ ″ 664 671 8 QAKQAFTF ″ B*1525 14 ″ 21 18 ″ ″ 664 671 8 QAKQAFTF ″ B*5802 3 ″ 5 18 ″ ″ 666 675 10 KQAFTFSPTY 563 A*2902 27 1,81 49 18 ″ ″ 666 675 10 KQAFTFSPTY ″ A*3002 30 ″ 53 18 ″ ″ 666 675 10 KQAFTFSPTY ″ B*1501 89 ″ 161 18 ″ ″ 666 675 10 KQAFTFSPTY ″ B*1502 63 ″ 114 18 ″ ″ 666 675 10 KQAFTFSPTY ″ B*1525 85 ″ 153 18 ″ ″ 666 675 10 KQAFTFSPTY ″ B*5001 32 ″ 58 18 ″ ″ 667 675 9 QAFTFSPTY 564 A*2902 46 ″ 83 18 ″ ″ 667 675 9 QAFTFSPTY ″ A*3002 58 ″ 104 18 ″ ″ 667 675 9 QAFTFSPTY ″ B*1525 66 ″ 119 18 ″ ″ 667 675 9 QAFTFSPTY ″ B*3501 73 ″ 133 18 ″ ″ 667 675 9 QAFTFSPTY ″ B*5701 12 ″ 22 18 ″ ″ 668 675 8 AFTFSPTY 565 A*2902 60 ″ 109 18 ″ ″ 668 675 8 AFTFSPTY ″ A*3002 56 ″ 102 18 ″ ″ 666 676 11 KQAFTFSPTYK 566 A*0301 100 1,78 178 18 ″ ″ 666 676 11 KQAFTFSPTYK ″ A*1101 83 ″ 147 18 ″ ″ 666 676 11 KQAFTFSPTYK ″ A*3001 49 ″ 87 18 ″ ″ 666 676 11 KQAFTFSPTYK ″ A*7401 60 ″ 106 18 ″ ″ 667 676 10 QAFTFSPTYK 567 A*0301 64 ″ 114 18 ″ ″ 667 676 10 QAFTFSPTYK ″ A*1101 78 ″ 139 18 ″ ″ 667 676 10 QAFTFSPTYK ″ A*6801 91 ″ 162 18 ″ ″ 667 676 10 QAFTFSPTYK ″ A*7401 59 ″ 104 18 ″ ″ 669 676 8 FTFSPTYK 568 A*0301 98 ″ 175 18 ″ ″ 669 676 8 FTFSPTYK ″ A*1101 96 ″ 170 18 ″ ″ 669 676 8 FTFSPTYK ″ A*3101 25 ″ 45 18 ″ ″ 669 676 8 FTFSPTYK ″ A*3303 69 ″ 123 18 ″ ″ 669 676 8 FTFSPTYK ″ A*7401 99 ″ 176 18 ″ ″ 669 677 9 FTFSPTYKA 569 A*0201 2 1,62 4 18 ″ ″ 669 677 9 FTFSPTYKA ″ A*6802 47 ″ 76 18 ″ ″ 669 677 9 FTFSPTYKA ″ B*5601 36 ″ 58 18 ″ ″ 668 678 11 AFTFSPTYKAF 570 A*2402 14 0,94 13 18 ″ ″ 669 678 10 FTFSPTYKAF 571 A*0101 64 ″ 60 18 ″ ″ 669 678 10 FTFSPTYKAF ″ A*2501 96 ″ 90 18 ″ ″ 669 678 10 FTFSPTYKAF ″ A*2601 92 ″ 87 18 ″ ″ 669 678 10 FTFSPTYKAF ″ B*1501 88 ″ 82 18 ″ ″ 669 678 10 FTFSPTYKAF ″ B*1502 100 ″ 94 18 ″ ″ 669 678 10 FTFSPTYKAF ″ B*1525 83 ″ 78 18 ″ ″ 669 678 10 FTFSPTYKAF ″ B*3501 36 ″ 34 18 ″ ″ 669 678 10 FTFSPTYKAF ″ B*3503 43 ″ 41 18 ″ ″ 669 678 10 FTFSPTYKAF ″ B*4601 98 ″ 92 18 ″ ″ 669 678 10 FTFSPTYKAF ″ B*5802 48 ″ 45 18 ″ ″ 670 678 9 TFSPTYKAF 572 A*2301 83 ″ 78 18 ″ ″ 670 678 9 TFSPTYKAF ″ A*2402 42 ″ 39 18 ″ ″ 669 679 11 FTFSPTYKAFL 573 A*2501 61 0,51 32 18 ″ ″ 669 679 11 FTFSPTYKAFL ″ A*2601 46 ″ 24 18 ″ ″ 669 679 11 FTFSPTYKAFL ″ B*4601 61 ″ 31 18 ″ ″ 672 679 8 SPTYKAFL 574 B*0801 39 ″ 20 18 ″ ″ 672 679 8 SPTYKAFL ″ B*3503 15 ″8 18 ″″ ″ ″ 672 679 8 SPTYKAFL ″ B*5501 1 ″ 1 18 ″ ″ 673 681 9 PTYKAFLSK 575 A*0301 72 1,52 110 18 ″ ″ 673 681 9 PTYKAFLSK ″ A*1101 61 ″ 92 18 ″ ″ 674 681 8 TYKAFLSK 576 A*3001 77 ″ 117 18 ″ ″ 674 681 8 TYKAFLSK ″ A*3101 18 ″ 27 18 ″ ″ 673 683 11 PTYKAFLSKQY 577 A*0101 47 1,56 73 18 ″ ″ 673 683 11 PTYKAFLSKQY ″ A*2902 8 ″ 12 18 ″ ″ 673 683 11 PTYKAFLSKQY ″ A*3002 27 ″ 42 18 ″ ″ 674 683 10 TYKAFLSKQY 578 A*2902 67 ″ 104 18 ″ ″ 674 683 10 TYKAFLSKQY ″ A*3002 21 ″ 33 18 ″ ″ 676 683 8 KAFLSKQY 579 A*3002 51 ″ 79 18 ″ ″ 676 683 8 KAFLSKQY ″ B*1501 25 ″ 39 18 ″ ″ 676 683 8 KAFLSKQY ″ B*1502 11 ″ 17 18 ″ ″ 676 683 8 KAFLSKQY ″ B*1525 61 ″ 95 18 ″ ″ 676 683 8 KAFLSKQY ″ B*5701 71 ″ 111 18 ″ ″ 676 683 8 KAFLSKQY ″ B*5801 51 ″ 79 18 ″ ″ 676 683 8 KAFLSKQY ″ B*5802 62 ″ 97 18 ″ ″ 676 684 9 KAFLSKQYM 580 B*5701 82 1,51 124 18 ″ ″ 676 684 9 KAFLSKQYM ″ B*5801 46 ″ 69 18 ″ ″ 676 685 10 KAFLSKQYMN 581 A*3001 63 ″ 24 18 ″ ″ 676 686 11 KAFLSKQYMNL 582 A*3001 48 1,83 88 18 ″ ″ 676 686 11 KAFLSKQYMNL ″ A*3201 24 ″ 44 18 ″ ″ 676 686 11 KAFLSKQYMNL ″ B*4801 13 ″ 25 18 ″ ″ 676 686 11 KAFLSKQYMNL ″ B*5701 62 ″ 114 18 ″ ″ 676 686 11 KAFLSKQYMNL ″ B*5801 19 ″ 34 18 ″ ″ 676 686 11 KAFLSKQYMNL ″ B*5802 23 ″ 43 18 ″ ″ 678 686 9 FLSKQYMNL 583 A*0201 33 ″ 61 18 ″ ″ 677 687 11 AFLSKQYMNLY 584 A*2902 84 1,58 133 18 ″ ″ 677 687 11 AFLSKQYMNLY ″ A*3002 55 ″ 87 18 ″ ″ 678 687 10 FLSKQYMNLY 585 A*0101 98 ″ 155 18 ″ ″ 678 687 10 FLSKQYMNLY ″ A*2501 67 ″ 106 18 ″ ″ 678 687 10 FLSKQYMNLY ″ A*3002 34 ″ 53 18 ″ ″ 678 687 10 FLSKQYMNLY ″ B*1501 23 ″ 37 18 ″ ″ 678 687 10 FLSKQYMNLY ″ B*1502 35 ″ 56 18 ″ ″ 678 687 10 FLSKQYMNLY ″ B*4601 18 ″ 28 18 ″ ″ 679 687 9 LSKQYMNLY 586 A*0101 96 ″ 152 18 ″ ″ 679 687 9 LSKQYMNLY ″ A*3002 69 ″ 109 18 ″ ″ 679 687 9 LSKQYMNLY ″ B*1501 27 ″ 42 18 ″ ″ 680 687 8 SKQYMNLY 587 B*3501 21 ″ 34 18 ″ ″ 679 689 11 LSKQYMNLYPV 588 B*0801 37 0,93 35 18 ″ ″ 681 689 9 KQYMNLYPV 589 A*0201 89 ″ 83 18 ″ ″ 681 689 9 KQYMNLYPV ″ A*0206 96 ″ 89 18 ″ ″ 681 689 9 KQYMNLYPV ″ A*3201 44 ″ 41 18 ″ ″ 681 689 9 KQYMNLYPV ″ B*1301 72 ″ 67 18 ″ ″ 681 689 9 KQYMNLYPV ″ B*1302 38 ″ 35 18 ″ ″ 681 689 9 KQYMNLYPV ″ B*1525 29 ″ 27 18 ″ ″ 681 689 9 KQYMNLYPV ″ B*2702 48 ″ 45 18 ″ ″ 681 689 9 KQYMNLYPV ″ B*4801 88 ″ 82 18 ″ ″ 681 689 9 KQYMNLYPV ″ B*5001 48 ″ 45 18 ″ ″ 681 689 9 KQYMNLYPV ″ B*5201 73 ″ 67 18 ″ ″ 682 689 8 QYMNLYPV 590 A*2301 59 ″ 54 18 ″ ″ 682 689 8 QYMNLYPV ″ A*2402 61 ″ 57 18 ″ ″ 681 690 10 KQYMNLYPVA 591 B*1302 3 1,25 4 18 ″ ″ 681 690 10 KQYMNLYPVA ″ B*4801 42 ″ 53 18 ″ ″ 681 690 10 KQYMNLYPVA ″ B*5001 16 ″ 20 18 ″ ″ 681 691 11 KQYMNLYPVAR 592 A*0301 49 1,78 88 18 ″ ″ 681 691 11 KQYMNLYPVAR ″ A*3101 100 ″ 178 18 ″ ″ 681 691 11 KQYMNLYPVAR ″ A*3201 23 ″ 40 18 ″ ″ 681 691 11 KQYMNLYPVAR ″ A*7401 100 ″ 178 18 ″ ″ 682 691 10 QYMNLYPVAR 593 A*3101 84 ″ 149 18 ″ ″ 682 691 10 QYMNLYPVAR ″ A*3303 90 ″ 160 18 ″ ″ 683 691 9 YMNLYPVAR 594 A*3101 78 ″ 140 18 ″ ″ 683 691 9 YMNLYPVAR ″ A*3303 89 ″ 158 18 ″ ″ 683 691 9 YMNLYPVAR ″ A*7401 94 ″ 167 18 ″ ″ 684 691 8 MNLYPVAR 595 A*3101 16 ″ 29 18 ″ ″ 684 691 8 MNLYPVAR ″ A*3303 75 ″ 133 18 ″ ″ Cumulative Class I-BCI score: 12576 657 665 9 MPLYACIQA 556 B*3501 44 1,41 62 19 657 691 657 665 9 MPLYACIQA ″ B*3503 49 ″ 68 19 ″ ″ 657 665 9 MPLYACIQA ″ B*5101 80 ″ 112 19 ″ ″ 657 665 9 MPLYACIQA ″ B*5501 93 ″ 131 19 ″ ″ 657 665 9 MPLYACIQA ″ B*5601 99 ″ 139 19 ″ ″ 657 666 10 MPLYACIQAK 557 B*3501 43 1,01 43 19 ″ ″ 657 666 10 MPLYACIQAK ″ B*5601 3 ″ 3 19 ″ ″ 658 666 9 PLYACIQAK 558 A*0301 74 ″ 75 19 ″ ″ 659 669 11 LYACIQAKQAF 559 A*2301 86 1,07 92 19 ″ ″ 659 669 11 LYACIQAKQAF ″ A*2402 88 ″ 94 19 ″ ″ 660 669 10 YACIQAKQAF 560 B*1502 26 ″ 28 19 ″ ″ 663 671 9 IQAKQAFTF 561 A*2402 84 1,58 133 19 ″ ″ 663 671 9 IQAKQAFTF ″ B*1301 61 ″ 96 19 ″ ″ 663 671 9 IQAKQAFTF ″ B*1501 63 ″ 99 19 ″ ″ 663 671 9 IQAKQAFTF ″ B*1525 71 ″ 112 19 ″ ″ 664 671 8 QAKQAFTF 562 B*1501 8 ″ 12 19 ″ ″ 664 671 8 QAKQAFTF ″ B*1502 37 ″ 59 19 ″ ″ 664 671 8 QAKQAFTF ″ B*1525 14 ″ 21 19 ″ ″ 664 671 8 QAKQAFTF ″ B*5802 3 ″ 5 19 ″ ″ 666 675 10 KQAFTFSPTY 563 A*2902 27 1,81 49 19 ″ ″ 666 675 10 KQAFTFSPTY ″ A*3002 30 ″ 53 19 ″ ″ 666 675 10 KQAFTFSPTY ″ B*1501 89 ″ 161 19 ″ ″ 666 675 10 KQAFTFSPTY ″ B*1502 63 ″ 114 19 ″ ″ 666 675 10 KQAFTFSPTY ″ B*1525 85 ″ 153 19 ″ ″ 666 675 10 KQAFTFSPTY ″ B*5001 32 ″ 58 19 ″ ″ 667 675 9 QAFTFSPTY 564 A*2902 46 ″ 83 19 ″ ″ 667 675 9 QAFTFSPTY ″ A*3002 58 ″ 104 19 ″ ″ 667 675 9 QAFTFSPTY ″ B*1525 66 ″ 119 19 ″ ″ 667 675 9 QAFTFSPTY ″ B*3501 73 ″ 133 19 ″ ″ 667 675 9 QAFTFSPTY ″ B*5701 12 ″ 22 19 ″ ″ 668 675 8 AFTFSPTY 565 A*2902 60 ″ 109 19 ″ ″ 668 675 8 AFTFSPTY ″ A*3002 56 ″ 102 19 ″ ″ 666 676 11 KQAFTFSPTYK 566 A*0301 100 1,78 178 19 ″ ″ 666 676 11 KQAFTFSPTYK ″ A*1101 83 ″ 147 19 ″ ″ 666 676 11 KQAFTFSPTYK ″ A*3001 49 ″ 87 19 ″ ″ 666 676 11 KQAFTFSPTYK ″ A*7401 60 ″ 106 19 ″ ″ 667 676 10 QAFTFSPTYK 567 A*0301 64 ″ 114 19 ″ ″ 667 676 10 QAFTFSPTYK ″ A*1101 78 ″ 139 19 ″ ″ 667 676 10 QAFTFSPTYK ″ A*6801 91 ″ 162 19 ″ ″ 667 676 10 QAFTFSPTYK ″ A*7401 59 ″ 104 19 ″ ″ 669 676 8 FTFSPTYK 568 A*0301 98 ″ 175 19 ″ ″ 669 676 8 FTFSPTYK ″ A*1101 96 ″ 170 19 ″ ″ 669 676 8 FTFSPTYK ″ A*3101 25 ″ 45 19 ″ ″ 669 676 8 FTFSPTYK ″ A*3303 69 ″ 123 19 ″ ″ 669 676 8 FTFSPTYK ″ A*7401 99 ″ 176 19 ″ ″ 669 677 9 FTFSPTYKA 569 A*0201 2 1,62 4 19 ″ ″ 669 677 9 FTFSPTYKA ″ A*6802 47 ″ 76 19 ″ ″ 669 677 9 FTFSPTYKA ″ B*5601 36 ″ 58 19 ″ ″ 668 678 11 AFTFSPTYKAF 570 A*2402 14 0,94 13 19 ″ ″ 669 678 10 FTFSPTYKAF 571 A*0101 64 ″ 60 19 ″ ″ 669 678 10 FTFSPTYKAF ″ A*2501 96 ″ 90 19 ″ ″ 669 678 10 FTFSPTYKAF ″ A*2601 92 ″ 87 19 ″ ″ 669 678 10 FTFSPTYKAF ″ B*1501 88 ″ 82 19 ″ ″ 669 678 10 FTFSPTYKAF ″ B*1502 100 ″ 94 19 ″ ″ 669 678 10 FTFSPTYKAF ″ B*1525 83 ″ 78 19 ″ ″ 669 678 10 FTFSPTYKAF ″ B*3501 36 ″ 34 19 ″ ″ 669 678 10 FTFSPTYKAF ″ B*3503 43 ″ 41 19 ″ ″ 669 678 10 FTFSPTYKAF ″ B*4601 98 ″ 92 19 ″ ″ 669 678 10 FTFSPTYKAF ″ B*5802 48 ″ 45 19 ″ ″ 670 678 9 TFSPTYKAF 572 A*2301 83 ″ 78 19 ″ ″ 670 678 9 TFSPTYKAF ″ A*2402 42 ″ 39 19 ″ ″ 669 679 11 FTFSPTYKAFL 573 A*2501 61 0,51 32 19 ″ ″ 669 679 11 FTFSPTYKAFL ″ A*2601 46 ″ 24 19 ″ ″ 669 679 11 FTFSPTYKAFL ″ B*4601 61 ″ 31 19 ″ ″ 672 679 8 sPTYKAFL 574 B*0801 39 ″ 20 19 ″ ″ 672 679 8 sPTYKAFL ″ B*3503 15 ″8 19 ″″ ″ ″ 672 679 8 SPTYKAFL ″ B*5501 1 ″ 1 19 ″ ″ 673 681 9 PTYKAFLSK 575 A*0301 72 1,52 110 19 ″ ″ 673 681 9 PTYKAFLSK ″ A*1101 61 ″ 92 19 ″ ″ 674 681 8 TYKAFLSK 576 A*3001 77 ″ 117 19 ″ ″ 674 681 8 TYKAFLSK ″ A*3101 18 ″ 27 19 ″ ″ 673 683 11 PTYKAFLSKQY 577 A*0101 47 1,56 73 19 ″ ″ 673 683 11 PTYKAFLSKQY ″ A*2902 8 ″ 12 19 ″ ″ 673 683 11 PTYKAFLSKQY ″ A*3002 27 ″ 42 19 ″ ″ 674 683 10 TYKAFLSKQY 578 A*2902 67 ″ 104 19 ″ ″ 674 683 10 TYKAFLSKQY ″ A*3002 21 ″ 33 19 ″ ″ 676 683 8 KAFLSKQY 579 A*3002 51 ″ 79 19 ″ ″ 676 683 8 KAFLSKQY ″ B*1501 25 ″ 39 19 ″ ″ 676 683 8 KAFLSKQY ″ B*1502 11 ″ 17 19 ″ ″ 676 683 8 KAFLSKQY ″ B*1525 61 ″ 95 19 ″ ″ 676 683 8 KAFLSKQY ″ B*5701 71 ″ 111 19 ″ ″ 676 683 8 KAFLSKQY ″ B*5801 51 ″ 79 19 ″ ″ 676 683 8 KAFLSKQY ″ B*5802 62 ″ 97 19 ″ ″ 676 684 9 KAFLSKQYM 580 B*5701 82 1,51 124 19 ″ ″ 676 684 9 KAFLSKQYM ″ B*5801 46 ″ 69 19 ″ ″ 676 685 10 KAFLSKQYMN 581 A*3001 63 ″ 24 19 ″ ″ 676 686 11 KAFLSKQYMNL 582 A*3001 48 1,83 88 19 ″ ″ 676 686 11 KAFLSKQYMNL ″ A*3201 24 ″ 44 19 ″ ″ 676 686 11 KAFLSKQYMNL ″ B*4801 13 ″ 25 19 ″ ″ 676 686 11 KAFLSKQYMNL ″ B*5701 62 ″ 114 19 ″ ″ 676 686 11 KAFLSKQYMNL ″ B*5801 19 ″ 34 19 ″ ″ 676 686 11 KAFLSKQYMNL ″ B*5802 23 ″ 43 19 ″ ″ 678 686 9 FLSKQYMNL 583 A*0201 33 ″ 61 19 ″ ″ 677 687 11 AFLSKQYMNLY 584 A*2902 84 1,58 133 19 ″ ″ 677 687 11 AFLSKQYMNLY ″ A*3002 55 ″ 87 19 ″ ″ 678 687 10 FLSKQYMNLY 585 A*0101 98 ″ 155 19 ″ ″ 678 687 10 FLSKQYMNLY ″ A*2501 67 ″ 106 19 ″ ″ 678 687 10 FLSKQYMNLY ″ A*3002 34 ″ 53 19 ″ ″ 678 687 10 FLSKQYMNLY ″ B*1501 23 ″ 37 19 ″ ″ 678 687 10 FLSKQYMNLY ″ B*1502 35 ″ 56 19 ″ ″ 678 687 10 FLSKQYMNLY ″ B*4601 18 ″ 28 19 ″ ″ 679 687 9 LSKQYMNLY 586 A*0101 96 ″ 152 19 ″ ″ 679 687 9 LSKQYMNLY ″ A*3002 69 ″ 109 19 ″ ″ 679 687 9 LSKQYMNLY ″ B*1501 27 ″ 42 19 ″ ″ 680 687 8 SKQYMNLY 587 B*3501 21 ″ 34 19 ″ ″ 679 689 11 LSKQYMNLYPV 588 B*0801 37 0,93 35 19 ″ ″ 681 689 9 KQYMNLYPV 589 A*0201 89 ″ 83 19 ″ ″ 681 689 9 KQYMNLYPV ″ A*0206 96 ″ 89 19 ″ ″ 681 689 9 KQYMNLYPV ″ A*3201 44 ″ 41 19 ″ ″ 681 689 9 KQYMNLYPV ″ B*1301 72 ″ 67 19 ″ ″ 681 689 9 KQYMNLYPV ″ B*1302 38 ″ 35 19 ″ ″ 681 689 9 KQYMNLYPV ″ B*1525 29 ″ 27 19 ″ ″ 681 689 9 KQYMNLYPV ″ B*2702 48 ″ 45 19 ″ ″ 681 689 9 KQYMNLYPV ″ B*4801 88 ″ 82 19 ″ ″ 681 689 9 KQYMNLYPV ″ B*5001 48 ″ 45 19 ″ ″ 681 689 9 KQYMNLYPV ″ B*5201 73 ″ 67 19 ″ ″ 682 689 8 QYMNLYPV 590 A*2301 59 ″ 54 19 ″ ″ 682 689 8 QYMNLYPV ″ A*2402 61 ″ 57 19 ″ ″ 681 690 10 KQYMNLYPVA 591 B*1302 3 1,25 4 19 ″ ″ 681 690 10 KQYMNLYPVA ″ B*4801 42 ″ 53 19 ″ ″ 681 690 10 KQYMNLYPVA ″ B*5001 16 ″ 20 19 ″ ″ 681 691 11 KQYMNLYPVAR 592 A*0301 49 1,78 88 19 ″ ″ 681 691 11 KQYMNLYPVAR ″ A*3101 100 ″ 178 19 ″ ″ 681 691 11 KQYMNLYPVAR ″ A*3201 23 ″ 40 19 ″ ″ 681 691 11 KQYMNLYPVAR ″ A*7401 100 ″ 178 19 ″ ″ 682 691 10 QYMNLYPVAR 593 A*3101 84 ″ 149 19 ″ ″ 682 691 10 QYMNLYPVAR ″ A*3303 90 ″ 160 19 ″ ″ 683 691 9 YMNLYPVAR 594 A*3101 78 ″ 140 19 ″ ″ 683 691 9 YMNLYPVAR ″ A*3303 89 ″ 158 19 ″ ″ 683 691 9 YMNLYPVAR ″ A*7401 94 ″ 167 19 ″ ″ 684 691 8 MNLYPVAR 595 A*3101 16 ″ 29 19 ″ ″ 684 691 8 MNLYPVAR ″ A*3303 75 ″ 133 19 ″ ″ Cumulative Class I-BCI score: 10420 716 723 8 RMRGTFVA 596 A*3001 92 1,41 130 20 715 746 716 724 9 RMRGTFVAP 597 A*3001 7 0,12 1 20 ″ ″ 717 724 8 MRGTFVAP 598 A*0206 94 ″ 11 20 ″ ″ 715 725 11 QRMRGTFVAPL 599 B*1402 89 0,99 88 20 ″ ″ 715 725 11 QRMRGTFVAPL ″ B*2702 83 ″ 82 20 ″ ″ 715 725 11 QRMRGTFVAPL ″ B*3801 57 ″ 57 20 ″ ″ 715 725 11 QRMRGTFVAPL ″ B*3901 99 ″ 98 20 ″ ″ 715 725 11 QRMRGTFVAPL ″ B*4801 29 ″ 29 20 ″ ″ 716 725 10 RMRGTFVAPL 600 B*0801 76 ″ 76 20 ″ ″ 716 725 10 RMRGTFVAPL ″ B*1402 65 ″ 64 20 ″ ″ 716 725 10 RMRGTFVAPL ″ B*1501 67 ″ 67 20 ″ ″ 716 725 10 RMRGTFVAPL ″ B*1525 47 ″ 47 20 ″ ″ 716 725 10 RMRGTFVAPL ″ B*4801 90 ″ 90 20 ″ ″ 717 725 9 MRGTFVAPL 601 B*1402 88 ″ 87 20 ″ ″ 717 725 9 MRGTFVAPL ″ B*2702 71 ″ 70 20 ″ ″ 717 725 9 MRGTFVAPL ″ B*3901 81 ″ 80 20 ″ ″ 716 726 11 RMRGTFVAPLP 602 A*3001 37 0,08 3 20 ″ ″ 718 726 9 RGTFVAPLP 603 B*5802 45 ″ 4 20 ″ ″ 717 727 11 MRGTFVAPLPI 604 B*1402 70 0,98 68 20 ″ ″ 717 727 11 MRGTFVAPLPI ″ B*2702 82 ″ 80 20 ″ ″ 717 727 11 MRGTFVAPLPI ″ B*3801 37 ″ 36 20 ″ ″ 717 727 11 MRGTFVAPLPI ″ B*3901 49 ″ 48 20 ″ ″ 717 727 11 MRGTFVAPLPI ″ B*5201 18 ″ 17 20 ″ ″ 719 727 9 GTFVAPLPI 605 A*3201 70 ″ 68 20 ″ ″ 719 727 9 GTFVAPLPI ″ B*5201 59 ″ 58 20 ″ ″ 720 727 8 TFVAPLPI 606 A*2301 19 ″ 19 20 ″ ″ 720 727 8 TFVAPLPI ″ A*2402 12 ″ 12 20 ″ ″ 719 728 10 GTFVAPLPIH 607 A*3001 97 0,37 36 20 ″ ″ 721 730 10 FVAPLPIHTA 608 A*0206 58 1,82 106 20 ″ ″ 721 730 10 FVAPLPIHTA ″ B*5601 51 ″ 94 20 ″ ″ 723 730 8 APLPIHTA 609 B*5501 67 ″ 123 20 ″ ″ 723 730 8 APLPIHTA ″ B*5601 76 ″ 138 20 ″ ″ 723 732 10 APLPIHTAEL 610 B*0702 67 1,48 99 20 ″ ″ 723 732 10 APLPIHTAEL ″ B*1402 69 ″ 102 20 ″ ″ 723 732 10 APLPIHTAEL ″ B*3503 66 ″ 98 20 ″ ″ 723 732 10 APLPIHTAEL ″ B*5501 53 ″ 79 20 ″ ″ 723 732 10 APLPIHTAEL ″ B*5601 44 ″ 65 20 ″ ″ 725 732 8 LPIHTAEL 611 B*1402 76 ″ 112 20 ″ ″ 725 732 8 LPIHTAEL ″ B*3503 89 ″ 132 20 ″ ″ 725 732 8 LPIHTAEL ″ B*3901 48 ″ 71 20 ″ ″ 725 732 8 LPIHTAEL ″ B*5101 88 ″ 131 20 ″ ″ 725 732 8 LPIHTAEL ″ B*5301 77 ″ 114 20 ″ ″ 725 732 8 LPIHTAEL ″ B*5501 74 ″ 110 20 ″ ″ 725 732 8 LPIHTAEL ″ B*5601 71 ″ 104 20 ″ ″ 723 733 11 APLPIHTAELL 612 B*0702 33 1,70 57 20 ″ ″ 723 733 11 APLPIHTAELL ″ B*1402 39 ″ 67 20 ″ ″ 725 733 9 LPIHTAELL 613 B*0702 1 ″ 2 20 ″ ″ 725 733 9 LPIHTAELL ″ B*1402 38 ″ 65 20 ″ ″ 725 733 9 LPIHTAELL ″ B*3503 57 ″ 97 20 ″ ″ 725 733 9 LPIHTAELL ″ B*5101 78 ″ 133 20 ″ ″ 725 733 9 LPIHTAELL ″ B*5301 61 ″ 103 20 ″ ″ 725 733 9 LPIHTAELL ″ B*5501 10 ″ 18 20 ″ ″ 725 733 9 LPIHTAELL ″ B*5601 26 ″ 44 20 ″ ″ 725 734 10 LPIHTAELLA 614 B*3503 42 1,12 47 20 ″ ″ 725 734 10 LPIHTAELLA ″ B*5501 81 ″ 91 20 ″ ″ 725 734 10 LPIHTAELLA ″ B*5601 92 ″ 103 20 ″ ″ 725 735 11 LPIHTAELLAA 615 B*0702 45 1,10 49 20 ″ ″ 725 735 11 LPIHTAELLAA ″ B*3501 76 ″ 84 20 ″ ″ 725 735 11 LPIHTAELLAA ″ B*3503 65 ″ 71 20 ″ ″ 725 735 11 LPIHTAELLAA ″ B*5101 45 ″ 49 20 ″ ″ 725 735 11 LPIHTAELLAA ″ B*5501 92 ″ 101 20 ″ ″ 725 735 11 LPIHTAELLAA ″ B*5601 97 ″ 107 20 ″ ″ 728 735 8 HTAELLAA 616 A*2501 31 ″ 34 20 ″ ″ 728 735 8 HTAELLAA ″ A*2601 72 ″ 79 20 ″ ″ 728 735 8 HTAELLAA ″ B*5501 9 ″ 10 20 ″ ″ 728 735 8 HTAELLAA ″ B*5601 32 ″ 35 20 ″ ″ 728 736 9 HTAELLAAC 617 A*2501 86 0,20 18 20 ″ ″ 728 736 9 HTAELLAAC ″ A*2601 54 ″ 11 20 ″ ″ 728 737 10 HTAELLAACF 618 A*0101 32 1,63 52 20 ″ ″ 728 737 10 HTAELLAACF ″ A*2501 94 ″ 153 20 ″ ″ 728 737 10 HTAELLAACF ″ A*2601 85 ″ 138 20 ″ ″ 728 737 10 HTAELLAACF ″ B*1502 43 ″ 69 20 ″ ″ 728 737 10 HTAELLAACF ″ B*4601 72 ″ 117 20 ″ ″ 728 737 10 HTAELLAACF ″ B*5802 42 ″ 68 20 ″ ″ 730 737 8 AELLAACF 619 B*1301 65 ″ 105 20 ″ ″ 730 737 8 AELLAACF ″ B*1801 76 ″ 124 20 ″ ″ 730 737 8 AELLAACF ″ B*4001 70 ″ 113 20 ″ ″ 730 737 8 AELLAACF ″ B*4002 65 ″ 106 20 ″ ″ 730 737 8 AELLAACF ″ B*4403 96 ″ 156 20 ″ ″ 730 737 8 AELLAACF ″ B*4901 52 ″ 85 20 ″ ″ 730 737 8 AELLAACF ″ B*5001 40 ″ 65 20 ″ ″ 728 738 11 HTAELLAACFA 620 A*2601 36 0,81 29 20 ″ ″ 730 738 9 AELLAACFA 621 B*1301 59 ″ 48 20 ″ ″ 730 738 9 AELLAACFA ″ B*1302 10 ″ 8 20 ″ ″ 730 738 9 AELLAACFA ″ B*3701 29 ″ 23 20 ″ ″ 730 738 9 AELLAACFA ″ B*4002 85 ″ 69 20 ″ ″ 730 738 9 AELLAACFA ″ B*4402 73 ″ 59 20 ″ ″ 730 738 9 AELLAACFA ″ B*4403 68 ″ 55 20 ″ ″ 730 738 9 AELLAACFA ″ B*4901 65 ″ 53 20 ″ ″ 730 738 9 AELLAACFA ″ B*5001 72 ″ 59 20 ″ ″ 729 739 11 TAELLAACFAR 622 A*6801 54 1,51 82 20 ″ ″ 730 739 10 AELLAACFAR 623 B*4002 45 ″ 68 20 ″ ″ 731 739 9 ELLAACFAR 624 A*3303 80 ″ 121 20 ″ ″ 731 739 9 ELLAACFAR ″ A*6801 71 ″ 107 20 ″ ″ 731 739 9 ELLAACFAR ″ A*7401 18 ″ 28 20 ″ ″ 732 739 8 LLAACFAR 625 A*3101 24 ″ 36 20 ″ ″ 732 739 8 LLAACFAR ″ A*3303 66 ″ 100 20 ″ ″ 732 739 8 LLAACFAR ″ A*6801 57 ″ 87 20 ″ ″ 732 739 8 LLAACFAR ″ A*7401 93 ″ 140 20 ″ ″ 730 740 11 AELLAACFARS 626 B*4402 12 0,24 3 20 ″ ″ 730 740 11 AELLAACFARS ″ B*4403 4 ″ 1 20 ″ ″ 733 740 8 LAACFARS 627 A*0206 13 ″ 3 20 ″ ″ 731 741 11 ELLAACFARSR 628 A*3303 37 1,17 43 20 ″ ″ 732 741 10 LLAACFARSR 629 A*3101 58 ″ 68 20 ″ ″ 732 741 10 LLAACFARSR ″ A*3303 6 ″ 7 20 ″ ″ 732 741 10 LLAACFARSR ″ A*7401 66 ″ 77 20 ″ ″ 733 741 9 LAACFARSR 630 A*3303 28 ″ 33 20 ″ ″ 733 741 9 LAACFARSR ″ A*6801 56 ″ 66 20 ″ ″ 734 741 8 AACFARSR 631 A*3101 15 ″ 18 20 ″ ″ 737 744 8 FARSRSGA 632 B*0801 85 0,75 63 20 ″ ″ 737 744 8 FARSRSGA ″ B*5501 59 ″ 44 20 ″ ″ 737 744 8 FARSRSGA ″ B*5601 1 ″ 1 20 ″ ″ 737 745 9 FARSRSGAK 633 A*3001 39 0,48 19 20 ″ ″ 737 745 9 FARSRSGAK ″ B*5501 16 ″ 8 20 ″ ″ 737 746 10 FARSRSGAKL 634 B*1402 25 1,60 41 20 ″ ″ 737 746 10 FARSRSGAKL ″ B*4601 3 ″ 5 20 ″ ″ 737 746 10 FARSRSGAKL ″ B*5501 15 ″ 24 20 ″ ″ 738 746 9 ARSRSGAKL 635 B*2702 12 ″ 19 20 ″ ″ 739 746 8 RSRSGAKL 636 A*3001 76 ″ 122 20 ″ ″ Cumulative BCI Class Iscore: 7869 754 762 9 VLsRKYTSF 638 B*0801 68 1,77 120 21 754 791 754 762 9 VLsRKYTSF ″ B*1501 17 ″ 30 21 ″ ″ 755 762 8 LSRKYTSF 639 B*0801 61 ″ 108 21 ″ ″ 755 762 8 LSRKYTSF ″ B*1501 98 ″ 174 21 ″ ″ 755 762 8 LSRKYTSF ″ B*1502 85 ″ 150 21 ″ ″ 755 762 8 LSRKYTSF ″ B*1525 81 ″ 144 21 ″ ″ 755 762 8 LSRKYTSF ″ B*4601 59 ″ 104 21 ″ ″ 755 762 8 LSRKYTSF ″ B*5701 61 ″ 107 21 ″ ″ 755 762 8 LSRKYTSF ″ B*5802 46 ″ 82 21 ″ ″ 754 764 11 VLSRKYTSFPW 640 A*3201 17 0,99 16 21 ″ ″ 754 764 11 VLSRKYTSFPW ″ B*5701 55 ″ 54 21 ″ ″ 754 764 11 VLSRKYTSFPW ″ B*5801 56 ″ 55 21 ″ ″ 754 764 11 VLSRKYTSFPW ″ B*5802 22 ″ 21 21 ″ ″ 755 764 10 LSRKYTSFPW 641 B*1525 10 ″ 10 21 ″ ″ 755 764 10 LSRKYTSFPW ″ B*5802 96 ″ 94 21 ″ ″ 756 764 9 SRKYTSFPW 642 B*2702 81 ″ 80 21 ″ ″ 757 764 8 RKYTSFPW 643 B*1301 52 ″ 51 21 ″ ″ 757 764 8 RKYTSFPW ″ B*2702 94 ″ 93 21 ″ ″ 757 764 8 RKYTSFPW ″ B*4402 4 ″ 4 21 ″ ″ 757 764 8 RKYTSFPW ″ B*4403 12 ″ 12 21 ″ ″ 757 764 8 RKYTSFPW ″ B*5701 3 ″ 3 21 ″ ″ 757 764 8 RKYTSFPW ″ B*5802 12 ″ 11 21 ″ ″ 755 765 11 LSRKYTSFPWL 644 A*3001 36 1,24 45 21 ″ ″ 755 765 11 LSRKYTSFPWL ″ B*0801 36 ″ 44 21 ″ ″ 756 765 10 SRKYTSFPWL 645 A*3001 21 ″ 26 21 ″ ″ 756 765 10 SRKYTSFPWL ″ B*1402 24 ″ 30 21 ″ ″ 756 765 10 SRKYTSFPWL ″ B*2702 46 ″ 57 21 ″ ″ 756 765 10 SRKYTSFPWL ″ B*2705 10 ″ 13 21 ″ ″ 757 765 9 RKYTSFPWL 646 B*1402 8 ″ 10 21 ″ ″ 757 765 9 RKYTSFPWL ″ B*2702 4 ″ 4 21 ″ ″ 757 765 9 RKYTSFPWL ″ B*4801 87 ″ 108 21 ″ ″ 758 765 8 KYTSFPWL 647 A*2301 81 ″ 101 21 ″ ″ 758 765 8 KYTSFPWL ″ A*2402 77 ″ 96 21 ″ ″ 756 766 11 SRKYTSFPWLL 648 B*1402 64 1,92 122 21 ″ ″ 756 766 11 SRKYTSFPWLL ″ B*2702 80 ″ 152 21 ″ ″ 756 766 11 SRKYTSFPWLL ″ B*3901 26 ″ 50 21 ″ ″ 757 766 10 RKYTSFPWLL 649 B*1302 8 ″ 16 21 ″ ″ 757 766 10 RKYTSFPWLL ″ B*1402 63 ″ 120 21 ″ ″ 757 766 10 RKYTSFPWLL ″ B*2702 70 ″ 134 21 ″ ″ 757 766 10 RKYTSFPWLL ″ B*3901 17 ″ 32 21 ″ ″ 757 766 10 RKYTSFPWLL ″ B*4801 75 ″ 144 21 ″ ″ 758 766 9 KYTSFPWLL 650 A*2301 97 ″ 185 21 ″ ″ 758 766 9 KYTSFPWLL ″ A*2402 96 ″ 185 21 ″ ″ 759 766 8 YTSFPWLL 651 A*0101 57 ″ 108 21 ″ ″ 759 766 8 YTSFPWLL ″ A*2601 18 ″ 34 21 ″ ″ 759 766 8 YTSFPWLL ″ B*5801 5 ″ 10 21 ″ ″ 757 767 11 RKYTSFPWLLG 652 B*2705 48 0,64 31 21 ″ ″ 758 767 10 KYTSFPWLLG 653 A*3201 11 ″ 7 21 ″ ″ 759 767 9 YTsFPWLLG 654 A*0101 9 ″ 6 21 ″ ″ 762 769 8 FPWLLGCT 655 B*3501 65 0,19 13 21 ″ ″ 762 769 8 FPWLLGCT ″ B*3503 8 ″ 2 21 ″ ″ 762 769 8 FPWLLGCT ″ B*5101 35 ″ 7 21 ″ ″ 762 769 8 FPWLLGCT ″ B*5501 66 ″ 13 21 ″ ″ 762 769 8 FPWLLGCT ″ B*5601 85 ″ 16 21 ″ ″ 762 770 9 FPWLLGCTA 656 B*1402 14 1,76 25 21 ″ ″ 762 770 9 FPWLLGCTA ″ B*3501 39 ″ 68 21 ″ ″ 762 770 9 FPWLLGCTA ″ B*3503 88 ″ 155 21 ″ ″ 762 770 9 FPWLLGCTA ″ B*5101 33 ″ 59 21 ″ ″ 762 771 10 FPWLLGCTAN 657 B*0702 7 0,39 3 21 ″ ″ 762 771 10 FPWLLGCTAN ″ B*3501 79 ″ 31 21 ″ ″ 762 771 10 FPWLLGCTAN ″ B*3503 24 ″ 9 21 ″ ″ 762 771 10 FPWLLGCTAN ″ B*5101 57 ″ 22 21 ″ ″ 762 771 10 FPWLLGCTAN ″ B*5301 52 ″ 20 21 ″ ″ 762 771 10 FPWLLGCTAN ″ B*5501 52 ″ 20 21 ″ ″ 762 771 10 FPWLLGCTAN ″ B*5601 69 ″ 27 21 ″ ″ 762 772 11 FPWLLGCTANW 658 B*1402 55 1,72 94 21 ″ ″ 762 772 11 FPWLLGCTANW ″ B*1801 48 ″ 82 21 ″ ″ 762 772 11 FPWLLGCTANW ″ B*3501 93 ″ 161 21 ″ ″ 762 772 11 FPWLLGCTANW ″ B*3503 81 ″ 140 21 ″ ″ 762 772 11 FPWLLGCTANW ″ B*3801 63 ″ 109 21 ″ ″ 762 772 11 FPWLLGCTANW ″ B*5101 87 ″ 149 21 ″ ″ 762 772 11 FPWLLGCTANW ″ B*5501 8 ″ 14 21 ″ ″ 762 772 11 FPWLLGCTANW ″ B*5601 50 ″ 86 21 ″ ″ 763 772 10 PWLLGCTANW 659 A*2301 67 ″ 116 21 ″ ″ 763 772 10 PWLLGCTANW ″ A*2402 32 ″ 54 21 ″ ″ 764 772 9 WLLGCTANW 660 B*5701 26 ″ 44 21 ″ ″ 764 773 10 WLLGcTANWI 661 A*0201 91 0,22 20 21 ″ ″ 765 773 9 LLGCTANWI 662 A*0201 71 ″ 15 21 ″ ″ 764 774 11 WLLGCTANWIL 663 B*3801 18 1,41 26 21 ″ ″ 764 774 11 WLLGCTANWIL ″ B*3901 74 ″ 104 21 ″ ″ 764 774 11 WLLGCTANWIL ″ B*4801 40 ″ 57 21 ″ ″ 765 774 10 LLGCtANWIL 664 A*0201 64 ″ 90 21 ″ ″ 765 775 11 LLGCTANWILR 665 A*7401 30 1,01 31 21 ″ ″ 766 775 10 LGCTANWILR 666 A*3201 33 ″ 34 21 ″ ″ 768 775 8 CTANWILR 667 A*1101 72 ″ 72 21 ″ ″ 768 775 8 CTANWILR ″ A*3101 53 ″ 54 21 ″ ″ 768 775 8 CTANWILR ″ A*3303 79 ″ 80 21 ″ ″ 768 775 8 CTANWILR ″ A*6801 94 ″ 95 21 ″ ″ 768 775 8 CTANWILR ″ A*7401 74 ″ 75 21 ″ ″ 769 779 11 TANWILRGTSF 668 B*1502 33 1,20 40 21 ″ ″ 769 779 11 TANWILRGTSF ″ B*3501 11 ″ 13 21 ″ ″ 769 779 11 TANWILRGTSF ″ B*4601 25 ″ 29 21 ″ ″ 769 779 11 TANWILRGTSF ″ B*5802 20 ″ 24 21 ″ ″ 770 779 10 ANWILRGTSF 669 B*4402 8 ″ 9 21 ″ ″ 771 779 9 NWILRGTSF 670 A*2301 2 ″ 2 21 ″ ″ 771 779 9 NWILRGTSF ″ A*2402 30 ″ 36 21 ″ ″ 772 779 8 WILRGTSF 671 B*0801 7 ″ 8 21 ″ ″ 772 779 8 WILRGTSF ″ B*1501 52 ″ 62 21 ″ ″ 772 779 8 WILRGTSF ″ B*1502 81 ″ 97 21 ″ ″ 772 779 8 WILRGTSF ″ B*1525 63 ″ 75 21 ″ ″ 772 779 8 WILRGTSF ″ B*4601 39 ″ 47 21 ″ ″ 772 780 9 WILRGTSFV 672 A*0201 100 1,19 119 21 ″ ″ 772 780 9 WILRGTSFV ″ A*0206 69 ″ 82 21 ″ ″ 771 781 11 NWILRGTSFVY 673 A*2902 51 1,69 86 21 ″ ″ 771 781 11 NWILRGTSFVY ″ B*1801 24 ″ 40 21 ″ ″ 772 781 10 WILRGTSFVY 674 B*1502 59 ″ 100 21 ″ ″ 772 781 10 WILRGTSFVY ″ B*1525 8 ″ 14 21 ″ ″ 772 781 10 WILRGTSFVY ″ B*4601 2 ″ 3 21 ″ ″ 773 781 9 ILRGTSFVY 675 A*0301 23 ″ 39 21 ″ ″ 773 781 9 ILRGTSFVY ″ A*2902 63 ″ 108 21 ″ ″ 773 781 9 ILRGTSFVY ″ A*3002 72 ″ 122 21 ″ ″ 773 781 9 ILRGTSFVY ″ B*1501 83 ″ 140 21 ″ ″ 773 781 9 ILRGTSFVY ″ B*1525 69 ″ 118 21 ″ ″ 774 781 8 LRGTSFVY 676 B*2702 23 ″ 39 21 ″ ″ 774 781 8 LRGTSFVY ″ B*2705 37 ″ 63 21 ″ ″ 773 782 10 ILRGTSFVYV 677 A*0201 71 1,67 119 21 ″ ″ 776 785 10 GTSFVYVPSA 678 A*3001 73 1,35 98 21 ″ ″ 776 785 10 GTSFVYVPSA ″ B*5701 45 ″ 61 21 ″ ″ 778 786 9 SFVYVPSAL 679 B*1402 7 1,57 11 21 ″ ″ 779 786 8 FVYVPSAL 680 A*2501 27 ″ 42 21 ″ ″ 779 786 8 FVYVPSAL ″ B*0801 5 ″ 8 21 ″ ″ 779 786 8 FVYVPSAL ″ B*1402 75 ″ 118 21 ″ ″ 779 786 8 FVYVPSAL ″ B*1502 54 ″ 85 21 ″ ″ 779 786 8 FVYVPSAL ″ B*3503 41 ″ 64 21 ″ ″ 779 786 8 FVYVPSAL ″ B*3801 41 ″ 64 21 ″ ″ 779 786 8 FVYVPSAL ″ B*3901 73 ″ 114 21 ″ ″ 779 786 8 FVYVPSAL ″ B*4601 77 ″ 121 21 ″ ″ 779 786 8 FVYVPSAL ″ B*5501 45 ″ 71 21 ″ ″ 779 786 8 FVYVPSAL ″ B*5601 24 ″ 38 21 ″ ″ 781 788 8 YVPSALNP 681 A*0206 73 0,38 27 21 ″ ″ 779 789 11 FVYVPSALNPA 682 A*6802 15 0,68 10 21 ″ ″ 779 789 11 FVYVPSALNPA ″ B*4601 67 ″ 46 21 ″ ″ 779 789 11 FVYVPSALNPA ″ B*5501 65 ″ 44 21 ″ ″ 779 789 11 FVYVPSALNPA ″ B*5601 74 ″ 51 21 ″ ″ 781 789 9 YVPSALNPA 683 A*0206 42 ″ 28 21 ″ ″ 782 789 8 VPSALNPA 684 B*0702 22 ″ 15 21 ″ ″ 782 789 8 VPSALNPA ″ B*3503 1 ″ 1 21 ″ ″ 782 789 8 VPSALNPA ″ B*5101 5 ″ 3 21 ″ ″ 782 789 8 VPSALNPA ″ B*5501 80 ″ 55 21 ″ ″ 782 789 8 VPSALNPA ″ B*5601 91 ″ 62 21 ″ ″ 781 790 10 YVPSALNPAD 685 A*3001 14 0,18 3 21 ″ ″ Cumulative Class I-BCI score: 8555 757 765 9 RKYTSFPWL 646 B*1402 8 1,24 10 22 757 792 757 765 9 RKYTSFPWL ″ B*2702 4 ″ 4 22 ″ ″ 757 765 9 RKYTSFPWL ″ B*4801 87 ″ 108 22 ″ ″ 758 765 8 KYTSFPWL 647 A*2301 81 ″ 101 22 ″ ″ 758 765 8 KYTSFPWL ″ A*2402 77 ″ 96 22 ″ ″ 756 766 11 sRKYTSFPWLL 648 B*1402 64 1,92 122 22 ″ ″ 756 766 11 sRKYTSFPWLL ″ B*2702 80 ″ 152 22 ″ ″ 756 766 11 sRKYTSFPWLL ″ B*3901 26 ″ 50 22 ″ ″ 757 766 10 RKYTSFPWLL 649 B*1302 8 ″ 16 22 ″ ″ 757 766 10 RKYTSFPWLL ″ B*1402 63 ″ 120 22 ″ ″ 757 766 10 RKYTSFPWLL ″ B*2702 70 ″ 134 22 ″ ″ 757 766 10 RKYTSFPWLL ″ B*3901 17 ″ 32 22 ″ ″ 757 766 10 RKYTSFPWLL ″ B*4801 75 ″ 144 22 ″ ″ 758 766 9 KYTSFPWLL 650 A*2301 97 ″ 185 22 ″ ″ 758 766 9 KYTSFPWLL ″ A*2402 96 ″ 185 22 ″ ″ 759 766 8 YTSFPWLL 651 A*0101 57 ″ 108 22 ″ ″ 759 766 8 YTSFPWLL ″ A*2601 18 ″ 34 22 ″ ″ 759 766 8 YTSFPWLL ″ B*5801 5 ″ 10 22 ″ ″ 757 767 11 RKYTSFPWLLG 652 B*2705 48 0,64 31 22 ″ ″ 758 767 10 KYTSFPWLLG 653 A*3201 11 ″ 7 22 ″ ″ 759 767 9 YTsFPWLLG 654 A*0101 9 ″ 6 22 ″ ″ 762 769 8 FPWLLGCT 655 B*3501 65 0,19 13 22 ″ ″ 762 769 8 FPWLLGCT ″ B*3503 8 ″ 2 22 ″ ″ 762 769 8 FPWLLGCT ″ B*5101 35 ″ 7 22 ″ ″ 762 769 8 FPWLLGCT ″ B*5501 66 ″ 13 22 ″ ″ 762 769 8 FPWLLGCT ″ B*5601 85 ″ 16 22 ″ ″ 762 770 9 FPWLLGCTA 656 B*1402 14 1,76 25 22 ″ ″ 762 770 9 FPWLLGCTA ″ B*3501 39 ″ 68 22 ″ ″ 762 770 9 FPWLLGCTA ″ B*3503 88 ″ 155 22 ″ ″ 762 770 9 FPWLLGCTA ″ B*5101 33 ″ 59 22 ″ ″ 762 771 10 FPWLLGCTAN 657 B*0702 7 0,39 3 22 ″ ″ 762 771 10 FPWLLGCTAN ″ B*3501 79 ″ 31 22 ″ ″ 762 771 10 FPWLLGCTAN ″ B*3503 24 ″ 9 22 ″ ″ 762 771 10 FPWLLGCTAN ″ B*5101 57 ″ 22 22 ″ ″ 762 771 10 FPWLLGCTAN ″ B*5301 52 ″ 20 22 ″ ″ 762 771 10 FPWLLGCTAN ″ B*5501 52 ″ 20 22 ″ ″ 762 771 10 FPWLLGCTAN ″ B*5601 69 ″ 27 22 ″ ″ 762 772 11 FPWLLGCTANW 658 B*1402 55 1,72 94 22 ″ ″ 762 772 11 FPWLLGCTANW ″ B*1801 48 ″ 82 22 ″ ″ 762 772 11 FPWLLGCTANW ″ B*3501 93 ″ 161 22 ″ ″ 762 772 11 FPWLLGCTANW ″ B*3503 81 ″ 140 22 ″ ″ 762 772 11 FPWLLGCTANW ″ B*3801 63 ″ 109 22 ″ ″ 762 772 11 FPWLLGCTANW ″ B*5101 87 ″ 149 22 ″ ″ 762 772 11 FPWLLGCTANW ″ B*5501 8 ″ 14 22 ″ ″ 762 772 11 FPWLLGCTANW ″ B*5601 50 ″ 86 22 ″ ″ 763 772 10 PWLLGCTANW 659 A*2301 67 ″ 116 22 ″ ″ 763 772 10 PWLLGCTANW ″ A*2402 32 ″ 54 22 ″ ″ 764 772 9 WLLGCTANW 660 B*5701 26 ″ 44 22 ″ ″ 764 773 10 WLLGcTANWI 661 A*0201 91 0,22 20 22 ″ ″ 765 773 9 LLGCTANWI 662 A*0201 71 ″ 15 22 ″ ″ 764 774 11 WLLGCTANWIL 663 B*3801 18 1,41 26 22 ″ ″ 764 774 11 WLLGCTANWIL ″ B*3901 74 ″ 104 22 ″ ″ 764 774 11 WLLGCTANWIL ″ B*4801 40 ″ 57 22 ″ ″ 765 774 10 LLGCtANWIL 664 A*0201 64 ″ 90 22 ″ ″ 765 775 11 LLGCTANWILR 665 A*7401 30 1,01 31 22 ″ ″ 766 775 10 LGCTANWILR 666 A*3201 33 ″ 34 22 ″ ″ 768 775 8 CTANWILR 667 A*1101 72 ″ 72 22 ″ ″ 768 775 8 CTANWILR ″ A*3101 53 ″ 54 22 ″ ″ 768 775 8 CTANWILR ″ A*3303 79 ″ 80 22 ″ ″ 768 775 8 CTANWILR ″ A*6801 94 ″ 95 22 ″ ″ 768 775 8 CTANWILR ″ A*7401 74 ″ 75 22 ″ ″ 769 779 11 TANWILRGTSF 668 B*1502 33 1,20 40 22 ″ ″ 769 779 11 TANWILRGTSF ″ B*3501 11 ″ 13 22 ″ ″ 769 779 11 TANWILRGTSF ″ B*4601 25 ″ 29 22 ″ ″ 769 779 11 TANWILRGTSF ″ B*5802 20 ″ 24 22 ″ ″ 770 779 10 ANWILRGTSF 669 B*4402 8 ″ 9 22 ″ ″ 771 779 9 NWILRGTSF 670 A*2301 2 ″ 2 22 ″ ″ 771 779 9 NWILRGTSF ″ A*2402 30 ″ 36 22 ″ ″ 772 779 8 WILRGTSF 671 B*0801 7 ″ 8 22 ″ ″ 772 779 8 WILRGTSF ″ B*1501 52 ″ 62 22 ″ ″ 772 779 8 WILRGTSF ″ B*1502 81 ″ 97 22 ″ ″ 772 779 8 WILRGTSF ″ B*1525 63 ″ 75 22 ″ ″ 772 779 8 WILRGTSF ″ B*4601 39 ″ 47 22 ″ ″ 772 780 9 WILRGTSFV 672 A*0201 100 1,19 119 22 ″ ″ 772 780 9 WILRGTSFV ″ A*0206 69 ″ 82 22 ″ ″ 771 781 11 NWILRGTSFVY 673 A*2902 51 1,69 86 22 ″ ″ 771 781 11 NWILRGTSFVY ″ B*1801 24 ″ 40 22 ″ ″ 772 781 10 WILRGTSFVY 674 B*1502 59 ″ 100 22 ″ ″ 772 781 10 WILRGTSFVY ″ B*1525 8 ″ 14 22 ″ ″ 772 781 10 WILRGTSFVY ″ B*4601 2 ″ 3 22 ″ ″ 773 781 9 ILRGTSFVY 675 A*0301 23 ″ 39 22 ″ ″ 773 781 9 ILRGTSFVY ″ A*2902 63 ″ 108 22 ″ ″ 773 781 9 ILRGTSFVY ″ A*3002 72 ″ 122 22 ″ ″ 773 781 9 ILRGTSFVY ″ B*1501 83 ″ 140 22 ″ ″ 773 781 9 ILRGTSFVY ″ B*1525 69 ″ 118 22 ″ ″ 774 781 8 LRGTSFVY 676 B*2702 23 ″ 39 22 ″ ″ 774 781 8 LRGTSFVY ″ B*2705 37 ″ 63 22 ″ ″ 773 782 10 ILRGTSFVYV 677 A*0201 71 1,67 119 22 ″ ″ 776 785 10 GTSFVYVPSA 678 A*3001 73 1,35 98 22 ″ ″ 776 785 10 GTSFVYVPSA ″ B*5701 45 ″ 61 22 ″ ″ 778 786 9 SFVYVPSAL 679 B*1402 7 1,57 11 22 ″ ″ 779 786 8 FVYVPSAL 680 A*2501 27 ″ 42 22 ″ ″ 779 786 8 FVYVPSAL ″ B*0801 5 ″ 8 22 ″ ″ 779 786 8 FVYVPSAL ″ B*1402 75 ″ 118 22 ″ ″ 779 786 8 FVYVPSAL ″ B*1502 54 ″ 85 22 ″ ″ 779 786 8 FVYVPSAL ″ B*3503 41 ″ 64 22 ″ ″ 779 786 8 FVYVPSAL ″ B*3801 41 ″ 64 22 ″ ″ 779 786 8 FVYVPSAL ″ B*3901 73 ″ 114 22 ″ ″ 779 786 8 FVYVPSAL ″ B*4601 77 ″ 121 22 ″ ″ 779 786 8 FVYVPSAL ″ B*5501 45 ″ 71 22 ″ ″ 779 786 8 FVYVPSAL ″ B*5601 24 ″ 38 22 ″ ″ 781 788 8 YVPSALNP 681 A*0206 73 0,38 27 22 ″ ″ 779 789 11 FVYVPSALNPA 682 A*6802 15 0,68 10 22 ″ ″ 779 789 11 FVYVPSALNPA ″ B*4601 67 ″ 46 22 ″ ″ 779 789 11 FVYVPSALNPA ″ B*5501 65 ″ 44 22 ″ ″ 779 789 11 FVYVPSALNPA ″ B*5601 74 ″ 51 22 ″ ″ 781 789 9 YVPSALNPA 683 A*0206 42 ″ 28 22 ″ ″ 782 789 8 VPSALNPA 684 B*0702 22 ″ 15 22 ″ ″ 782 789 8 VPSALNPA ″ B*3503 1 ″ 1 22 ″ ″ 782 789 8 VPSALNPA ″ B*5101 5 ″ 3 22 ″ ″ 782 789 8 VPSALNPA ″ B*5501 80 ″ 55 22 ″ ″ 782 789 8 VPSALNPA ″ B*5601 91 ″ 62 22 ″ ″ 781 790 10 YVPSALNPAD 685 A*3001 14 0,18 3 22 ″ ″ Cumulative Class I-BCI score: 6817 754 762 9 VLSRKYTSF 638 B*0801 68 1,77 120 23 754 789 754 762 9 VLSRKYTSF ″ B*1501 17 ″ 30 23 ″ ″ 755 762 8 LSRKYTSF 639 B*0801 61 ″ 108 23 ″ ″ 755 762 8 LSRKYTSF ″ B*1501 98 ″ 174 23 ″ ″ 755 762 8 LSRKYTSF ″ B*1502 85 ″ 150 23 ″ ″ 755 762 8 LSRKYTSF ″ B*1525 81 ″ 144 23 ″ ″ 755 762 8 LSRKYTSF ″ B*4601 59 ″ 104 23 ″ ″ 755 762 8 LSRKYTSF ″ B*5701 61 ″ 107 23 ″ ″ 755 762 8 LSRKYTSF ″ B*5802 46 ″ 82 23 ″ ″ 754 764 11 VLSRKYTSFPW 640 A*3201 17 0,99 16 23 ″ ″ 754 764 11 VLSRKYTSFPW ″ B*5701 55 ″ 54 23 ″ ″ 754 764 11 VLSRKYTSFPW ″ B*5801 56 ″ 55 23 ″ ″ 754 764 11 VLSRKYTSFPW ″ B*5802 22 ″ 21 23 ″ ″ 755 764 10 LSRKYTSFPW 641 B*1525 10 ″ 10 23 ″ ″ 755 764 10 LSRKYTSFPW ″ B*5802 96 ″ 94 23 ″ ″ 756 764 9 SRKYTSFPW 642 B*2702 81 ″ 80 23 ″ ″ 757 764 8 RKYTSFPW 643 B*1301 52 ″ 51 23 ″ ″ 757 764 8 RKYTSFPW ″ B*2702 94 ″ 93 23 ″ ″ 757 764 8 RKYTSFPW ″ B*4402 4 ″ 4 23 ″ ″ 757 764 8 RKYTSFPW ″ B*4403 12 ″ 12 23 ″ ″ 757 764 8 RKYTSFPW ″ B*5701 3 ″ 3 23 ″ ″ 757 764 8 RKYTSFPW ″ B*5802 12 ″ 11 23 ″ ″ 755 765 11 LSRKYTSFPWL 644 A*3001 36 1,24 45 23 ″ ″ 755 765 11 LSRKYTSFPWL ″ B*0801 36 ″ 44 23 ″ ″ 756 765 10 SRKYTSFPWL 645 A*3001 21 ″ 26 23 ″ ″ 756 765 10 SRKYTSFPWL ″ B*1402 24 ″ 30 23 ″ ″ 756 765 10 SRKYTSFPWL ″ B*2702 46 ″ 57 23 ″ ″ 756 765 10 SRKYTSFPWL ″ B*2705 10 ″ 13 23 ″ ″ 757 765 9 RKYTSFPWL 646 B*1402 8 ″ 10 23 ″ ″ 757 765 9 RKYTSFPWL ″ B*2702 4 ″ 4 23 ″ ″ 757 765 9 RKYTSFPWL ″ B*4801 87 ″ 108 23 ″ ″ 758 765 8 KYTSFPWL 647 A*2301 81 ″ 101 23 ″ ″ 758 765 8 KYTSFPWL ″ A*2402 77 ″ 96 23 ″ ″ 756 766 11 SRKYTSFPWLL 648 B*1402 64 1,92 122 23 ″ ″ 756 766 11 SRKYTSFPWLL ″ B*2702 80 ″ 152 23 ″ ″ 756 766 11 SRKYTSFPWLL ″ B*3901 26 ″ 50 23 ″ ″ 757 766 10 RKYTSFPWLL 649 B*1302 8 ″ 16 23 ″ ″ 757 766 10 RKYTSFPWLL ″ B*1402 63 ″ 120 23 ″ ″ 757 766 10 RKYTSFPWLL ″ B*2702 70 ″ 134 23 ″ ″ 757 766 10 RKYTSFPWLL ″ B*3901 17 ″ 32 23 ″ ″ 757 766 10 RKYTSFPWLL ″ B*4801 75 ″ 144 23 ″ ″ 758 766 9 KYTSFPWLL 650 A*2301 97 ″ 185 23 ″ ″ 758 766 9 KYTSFPWLL ″ A*2402 96 ″ 185 23 ″ ″ 759 766 8 YTSFPWLL 651 A*0101 57 ″ 108 23 ″ ″ 759 766 8 YTSFPWLL ″ A*2601 18 ″ 34 23 ″ ″ 759 766 8 YTSFPWLL ″ B*5801 5 ″ 10 23 ″ ″ 757 767 11 RKYTSFPWLLG 652 B*2705 48 0,64 31 23 ″ ″ 758 767 10 KYTSFPWLLG 653 A*3201 11 ″ 7 23 ″ ″ 759 767 9 Yi'sFPWLLG 654 A*0101 9 ″ 6 23 ″ ″ 762 769 8 FPWLLGCT 655 B*3501 65 0,19 13 23 ″ ″ 762 769 8 FPWLLGCT ″ B*3503 8 ″ 2 23 ″ ″ 762 769 8 FPWLLGCT ″ B*5101 35 ″ 7 23 ″ ″ 762 769 8 FPWLLGCT ″ B*5501 66 ″ 13 23 ″ ″ 762 769 8 FPWLLGCT ″ B*5601 85 ″ 16 23 ″ ″ 762 770 9 FPWLLGCTA 656 B*1402 14 1,76 25 23 ″ ″ 762 770 9 FPWLLGCTA ″ B*3501 39 ″ 68 23 ″ ″ 762 770 9 FPWLLGCTA ″ B*3503 88 ″ 155 23 ″ ″ 762 770 9 FPWLLGCTA ″ B*5101 33 ″ 59 23 ″ ″ 762 771 10 FPWLLGCTAN 657 B*0702 7 0,39 3 23 ″ ″ 762 771 10 FPWLLGCTAN ″ B*3501 79 ″ 31 23 ″ ″ 762 771 10 FPWLLGCTAN ″ B*3503 24 ″ 9 23 ″ ″ 762 771 10 FPWLLGCTAN ″ B*5101 57 ″ 22 23 ″ ″ 762 771 10 FPWLLGCTAN ″ B*5301 52 ″ 20 23 ″ ″ 762 771 10 FPWLLGCTAN ″ B*5501 52 ″ 20 23 ″ ″ 762 771 10 FPWLLGCTAN ″ B*5601 69 ″ 27 23 ″ ″ 762 772 11 FPWLLGCTANW 658 B*1402 55 1,72 94 23 ″ ″ 762 772 11 FPWLLGCTANW ″ B*1801 48 ″ 82 23 ″ ″ 762 772 11 FPWLLGCTANW ″ B*3501 93 ″ 161 23 ″ ″ 762 772 11 FPWLLGCTANW ″ B*3503 81 ″ 140 23 ″ ″ 762 772 11 FPWLLGCTANW ″ B*3801 63 ″ 109 23 ″ ″ 762 772 11 FPWLLGCTANW ″ B*5101 87 ″ 149 23 ″ ″ 762 772 11 FPWLLGCTANW ″ B*5501 8 ″ 14 23 ″ ″ 762 772 11 FPWLLGCTANW ″ B*5601 50 ″ 86 23 ″ ″ 763 772 10 PWLLGCTANW 659 A*2301 67 ″ 116 23 ″ ″ 763 772 10 PWLLGCTANW ″ A*2402 32 ″ 54 23 ″ ″ 764 772 9 WLLGCTANW 660 B*5701 26 ″ 44 23 ″ ″ 764 773 10 WLLGcTANWI 661 A*0201 91 0,22 20 23 ″ ″ 765 773 9 LLGCTANWI 662 A*0201 71 ″ 15 23 ″ ″ 764 774 11 WLLGCTANWIL 663 B*3801 18 1,41 26 23 ″ ″ 764 774 11 WLLGCTANWIL ″ B*3901 74 ″ 104 23 ″ ″ 764 774 11 WLLGCTANWIL ″ B*4801 40 ″ 57 23 ″ ″ 765 774 10 LLGCtANWIL 664 A*0201 64 ″ 90 23 ″ ″ 765 775 11 LLGCTANWILR 665 A*7401 30 1,01 31 23 ″ ″ 766 775 10 LGCTANWILR 666 A*3201 33 ″ 34 23 ″ ″ 768 775 8 CTANWILR 667 A*1101 72 ″ 72 23 ″ ″ 768 775 8 CTANWILR ″ A*3101 53 ″ 54 23 ″ ″ 768 775 8 CTANWILR ″ A*3303 79 ″ 80 23 ″ ″ 768 775 8 CTANWILR ″ A*6801 94 ″ 95 23 ″ ″ 768 775 8 CTANWILR ″ A*7401 74 ″ 75 23 ″ ″ 769 779 11 TANWILRGTSF 668 B*1502 33 1,20 40 23 ″ ″ 769 779 11 TANWILRGTSF ″ B*3501 11 ″ 13 23 ″ ″ 769 779 11 TANWILRGTSF ″ B*4601 25 ″ 29 23 ″ ″ 769 779 11 TANWILRGTSF ″ B*5802 20 ″ 24 23 ″ ″ 770 779 10 ANWILRGTSF 669 B*4402 8 ″ 9 23 ″ ″ 771 779 9 NwiLRGTSF 670 A*2301 2 ″ 2 23 ″ ″ 771 779 9 NwiLRGTSF ″ A*2402 30 ″ 36 23 ″ ″ 772 779 8 WILRGTSF 671 B*0801 7 ″ 8 23 ″ ″ 772 779 8 WILRGTSF ″ B*1501 52 ″ 62 23 ″ ″ 772 779 8 WILRGTSF ″ B*1502 81 ″ 97 23 ″ ″ 772 779 8 WILRGTSF ″ B*1525 63 ″ 75 23 ″ ″ 772 779 8 WILRGTSF ″ B*4601 39 ″ 47 23 ″ ″ 772 780 9 WILRGTSFV 672 A*0201 100 1,19 119 23 ″ ″ 772 780 9 WILRGTSFV ″ A*0206 69 ″ 82 23 ″ ″ 771 781 11 NWILRGTSFVY 673 A*2902 51 1,69 86 23 ″ ″ 771 781 11 NWILRGTSFVY ″ B*1801 24 ″ 40 23 ″ ″ 772 781 10 WILRGTSFVY 674 B*1502 59 ″ 100 23 ″ ″ 772 781 10 WILRGTSFVY ″ B*1525 8 ″ 14 23 ″ ″ 772 781 10 WILRGTSFVY ″ B*4601 2 ″ 3 23 ″ ″ 773 781 9 ILRGTSFVY 675 A*0301 23 ″ 39 23 ″ ″ 773 781 9 ILRGTSFVY ″ A*2902 63 ″ 108 23 ″ ″ 773 781 9 ILRGTSFVY ″ A*3002 72 ″ 122 23 ″ ″ 773 781 9 ILRGTSFVY ″ B*1501 83 ″ 140 23 ″ ″ 773 781 9 ILRGTSFVY ″ B*1525 69 ″ 118 23 ″ ″ 774 781 8 LRGTSFVY 676 B*2702 23 ″ 39 23 ″ ″ 774 781 8 LRGTSFVY ″ B*2705 37 ″ 63 23 ″ ″ 773 782 10 ILRGTSFVYV 677 A*0201 71 1,67 119 23 ″ ″ 776 785 10 GTSFVYVPSA 678 A*3001 73 1,35 98 23 ″ ″ 776 785 10 GTSFVYVPSA ″ B*5701 45 ″ 61 23 ″ ″ 778 786 9 SFVYVPSAL 679 B*1402 7 1,57 11 23 ″ ″ 779 786 8 FVYVPSAL 680 A*2501 27 ″ 42 23 ″ ″ 779 786 8 FVYVPSAL ″ B*0801 5 ″ 8 23 ″ ″ 779 786 8 FVYVPSAL ″ B*1402 75 ″ 118 23 ″ ″ 779 786 8 FVYVPSAL ″ B*1502 54 ″ 85 23 ″ ″ 779 786 8 FVYVPSAL ″ B*3503 41 ″ 64 23 ″ ″ 779 786 8 FVYVPSAL ″ B*3801 41 ″ 64 23 ″ ″ 779 786 8 FVYVPSAL ″ B*3901 73 ″ 114 23 ″ ″ 779 786 8 FVYVPSAL ″ B*4601 77 ″ 121 23 ″ ″ 779 786 8 FVYVPSAL ″ B*5501 45 ″ 71 23 ″ ″ 779 786 8 FVYVPSAL ″ B*5601 24 ″ 38 23 ″ ″ 781 788 8 YVPSALNP 681 A*0206 73 0,38 27 23 ″ ″ 779 789 11 FVYVPSALNPA 682 A*6802 15 0,68 10 23 ″ ″ 779 789 11 FVYVPSALNPA ″ B*4601 67 ″ 46 23 ″ ″ 779 789 11 FVYVPSALNPA ″ B*5501 65 ″ 44 23 ″ ″ 779 789 11 FVYVPSALNPA ″ B*5601 74 ″ 51 23 ″ ″ 781 789 9 YVPSALNPA 683 A*0206 42 ″ 28 23 ″ ″ 782 789 8 VPSALNPA 684 B*0702 22 ″ 15 23 ″ ″ 782 789 8 VPSALNPA ″ B*3503 1 ″ 1 23 ″ ″ 782 789 8 VPSALNPA ″ B*5101 5 ″ 3 23 ″ ″ 782 789 8 VPSALNPA ″ B*5501 80 ″ 55 23 ″ ″ 782 789 8 VPSALNPA ″ B*5601 91 ″ 62 23 ″ ″ Cumulative Class I-BCI score: 8553 ″Start″ and ″End″ are relative to the amino acid sequence of HBV polymerase as depicted in SEQ ID NO: 1 ^(A)Peptide amino acid sequence. Each HLA class I binding peptide of HBV polymerase is listed separately for each HLA class I molecule to which it is predicted to bind, and can be listed multiple times for that reason. ^(B)Class I-B score. See Material and Methods (Examples section). ^(C)C-score. See Material and Methods (Examples section). ^(D)Class I-BCI score. See Material and Methods (Examples section). ^(E)Cumulative Class I-BCI score. See Material and Methods (Examples section).

TABLE 4b Predicted HLA class II-restricted CD4⁺ T cell epitopes contained in SLP sequences from HBV polymerase protein. HLA class II binding peptides in SLP sequence derived from HBV Polymerase SEQ HLA- Class Peptide of invention (SLP) ID DRB1 II-B SLP SLP Start End Sequence^(A) NO: molecule score^(B) SLP# Start End 1 15 MPLSYQHFRKLLLLD 686 *0701 79 1 1 30 1 15 MPLSYQHFRKLLLLD ″ *1101 86 1 ″ ″ 1 15 MPLSYQHFRKLLLLD ″ *1501 9 1 ″ ″ 2 16 PLSYQHFRKLLLLDD 687 *0701 40 1 ″ ″ 2 16 PLSYQHFRKLLLLDD ″ *1101 84 1 ″ ″ 2 16 PLSYQHFRKLLLLDD ″ *1501 4 1 ″ ″ 3 17 LSYQHFRKLLLLDDG 688 *0701 9 1 ″ ″ 3 17 LSYQHFRKLLLLDDG ″ *1101 83 1 ″ ″ 3 17 LSYQHFRKLLLLDDG ″ *1501 3 1 ″ ″ 4 18 SYQHFRKLLLLDDGT 689 *1101 81 1 ″ ″ 5 19 YQHFRKLLLLDDGTE 690 *1101 80 1 ″ ″ 6 20 QHFRKLLLLDDGTEA 691 *0301 31 1 ″ ″ 6 20 QHFRKLLLLDDGTEA ″ *1101 56 1 ″ ″ 7 21 HFRKLLLLDDGTEAG 692 *0301 30 1 ″ ″ 8 22 FRKLLLLDDGTEAGP 693 *0301 29 1 ″ ″ 9 23 RKLLLLDDGTEAGPL 694 *0301 27 1 ″ ″ 10 24 KLLLLDDGTEAGPLE 695 *0301 26 1 ″ ″ 11 25 LLLLDDGTEAGPLEE 696 *0301 24 1 ″ ″ Cumulative Class II-B score^(C): 780 55 69 THKVGNFTGLYSSTV 697 *0101 14 2 52 86 55 69 THKVGNFTGLYSSTV ″ *1501 54 2 ″ ″ 56 70 HKVGNFTGLYSSTVP 698 *0101 10 2 ″ ″ 56 70 HKVGNFTGLYSSTVP ″ *1501 51 2 ″ ″ 57 71 KVGNFTGLYSSTVPI 699 *0101 64 2 ″ ″ 57 71 KVGNFTGLYSSTVPI ″ *0105 78 2 ″ ″ 57 71 KVGNFTGLYSSTVPI ″ *0107 78 2 ″ ″ 57 71 KVGNFTGLYSSTVPI ″ *0401 11 2 ″ ″ 57 71 KVGNFTGLYSSTVPI ″ *0701 26 2 ″ ″ 57 71 KVGNFTGLYSSTVPI ″ *1501 47 2 ″ ″ 58 72 VGNFTGLYSSTVPIF 700 *0101 93 2 ″ ″ 58 72 VGNFTGLYSSTVPIF ″ *0105 88 2 ″ ″ 58 72 VGNFTGLYSSTVPIF ″ *0107 88 2 ″ ″ 58 72 VGNFTGLYSSTVPIF ″ *0301 14 2 ″ ″ 58 72 VGNFTGLYSSTVPIF ″ *0401 23 2 ″ ″ 58 72 VGNFTGLYSSTVPIF ″ *0701 34 2 ″ ″ 58 72 VGNFTGLYSSTVPIF ″ *1501 59 2 ″ ″ 59 73 GNFTGLYSSTVPIFN 701 *0101 80 2 ″ ″ 59 73 GNFTGLYSSTVPIFN ″ *0105 55 2 ″ ″ 59 73 GNFTGLYSSTVPIFN ″ *0107 55 2 ″ ″ 59 73 GNFTGLYSSTVPIFN ″ *0301 16 2 ″ ″ 59 73 GNFTGLYSSTVPIFN ″ *0401 24 2 ″ ″ 59 73 GNFTGLYSSTVPIFN ″ *0701 54 2 ″ ″ 60 74 NFTGLYSSTVPIFNP 702 *0101 57 2 ″ ″ 60 74 NFTGLYSSTVPIFNP ″ *0301 11 2 ″ ″ 60 74 NFTGLYSSTVPIFNP ″ *0401 16 2 ″ ″ 60 74 NFTGLYSSTVPIFNP ″ *0701 30 2 ″ ″ 61 75 FTGLYSSTVPIFNPE 703 *0101 43 2 ″ ″ 61 75 FTGLYSSTVPIFNPE ″ *0301 13 2 ″ ″ 61 75 FTGLYSSTVPIFNPE ″ *0401 19 2 ″ ″ 61 75 FTGLYSSTVPIFNPE ″ *0701 11 2 ″ ″ 62 76 TGLYSSTVPIFNPEW 704 *0301 7 2 ″ ″ Cumulative Class II-B score: 1323 103 117 VNEKRRLKLIMPARF 705 *0101 47 3 103 135 103 117 VNEKRRLKLIMPARF ″ *0102 33 3 ″ ″ 103 117 VNEKRRLKLIMPARF ″ *0104 8 3 ″ ″ 103 117 VNEKRRLKLIMPARF ″ *0106 50 3 ″ ″ 103 117 VNEKRRLKLIMPARF ″ *0301 36 3 ″ ″ 103 117 VNEKRRLKLIMPARF ″ *0701 17 3 ″ ″ 103 117 VNEKRRLKLIMPARF ″ *1301 7 3 ″ ″ 103 117 VNEKRRLKLIMPARF ″ *1501 64 3 ″ ″ 104 118 NEKRRLKLIMPARFY 706 *0101 53 3 ″ ″ 104 118 NEKRRLKLIMPARFY ″ *0102 83 3 ″ ″ 104 118 NEKRRLKLIMPARFY ″ *0104 78 3 ″ ″ 104 118 NEKRRLKLIMPARFY ″ *0106 83 3 ″ ″ 104 118 NEKRRLKLIMPARFY ″ *0701 27 3 ″ ″ 104 118 NEKRRLKLIMPARFY ″ *1301 64 3 ″ ″ 104 118 NEKRRLKLIMPARFY ″ *1501 76 3 ″ ″ 105 119 EKRRLKLIMPARFYP 707 *0101 46 3 ″ ″ 105 119 EKRRLKLIMPARFYP ″ *0102 93 3 ″ ″ 105 119 EKRRLKLIMPARFYP ″ *0104 85 3 ″ ″ 105 119 EKRRLKLIMPARFYP ″ *0106 85 3 ″ ″ 105 119 EKRRLKLIMPARFYP ″ *0701 3 3 ″ ″ 105 119 EKRRLKLIMPARFYP ″ *1101 8 3 ″ ″ 105 119 EKRRLKLIMPARFYP ″ *1301 61 3 ″ ″ 105 119 EKRRLKLIMPARFYP ″ *1501 71 3 ″ ″ 106 120 KRRLKLIMPARFYPT 708 *0101 49 3 ″ ″ 106 120 KRRLKLIMPARFYPT ″ *0102 100 3 ″ ″ 106 120 KRRLKLIMPARFYPT ″ *0103 4 3 ″ ″ 106 120 KRRLKLIMPARFYPT ″ *0104 100 3 ″ ″ 106 120 KRRLKLIMPARFYPT ″ *0105 45 3 ″ ″ 106 120 KRRLKLIMPARFYPT ″ *0106 93 3 ″ ″ 106 120 KRRLKLIMPARFYPT ″ *0107 45 3 ″ ″ 106 120 KRRLKLIMPARFYPT ″ *1101 25 3 ″ ″ 106 120 KRRLKLIMPARFYPT ″ *1301 71 3 ″ ″ 106 120 KRRLKLIMPARFYPT ″ *1501 73 3 ″ ″ 107 121 RRLKLIMPARFYPTH 709 *0101 44 3 ″ ″ 107 121 RRLKLIMPARFYPTH ″ *0102 80 3 ″ ″ 107 121 RRLKLIMPARFYPTH ″ *0104 88 3 ″ ″ 107 121 RRLKLIMPARFYPTH ″ *0106 78 3 ″ ″ 107 121 RRLKLIMPARFYPTH ″ *1301 32 3 ″ ″ 107 121 RRLKLIMPARFYPTH ″ *1501 69 3 ″ ″ 108 122 RLKLIMPARFYPTHT 710 *0102 53 3 ″ ″ 108 122 RLKLIMPARFYPTHT ″ *0104 53 3 ″ ″ 108 122 RLKLIMPARFYPTHT ″ *0106 60 3 ″ ″ 108 122 RLKLIMPARFYPTHT ″ *1501 41 3 ″ ″ 109 123 LKLIMPARFYPTHTK 711 *1501 40 3 ″ ″ 111 125 LIMPARFYPTHTKYL 712 *0701 93 3 ″ ″ 112 126 IMPARFYPTHTKYLP 713 *0701 91 3 ″ ″ 113 127 MPARFYPTHTKYLPL 714 *0701 96 3 ″ ″ 114 128 PARFYPTHTKYLPLD 715 *0701 94 3 ″ ″ 115 129 ARFYPTHTKYLPLDK 716 *0701 90 3 ″ ″ 116 130 RFYPTHTKYLPLDKG 717 *0701 86 3 ″ ″ 117 131 FYPTHTKYLPLDKGI 718 *0701 81 3 ″ ″ 121 135 HTKYLPLDKGIKPYY 719 *1101 23 3 ″ ″ Cumulative Class II-B score: 3070 121 135 HTKYLPLDKGIKPYY 719 *1101 23 4 118 150 122 136 TKYLPLDKGIKPYYP 720 *1101 21 4 ″ ″ 130 144 GIKPYYPDQVVNHYF 721 *0401 26 4 ″ ″ 131 145 IKPYYPDQVVNHYFQ 722 *0401 51 4 ″ ″ 132 146 KPYYPDQVVNHYFQT 723 *0401 21 4 ″ ″ Cumulative Class II-B score: 143 139 153 VVNHYFQTRHYLHTL 726 *1101 87 5 139 177 139 153 VVNHYFQTRHYLHTL ″ *1501 70 5 ″ ″ 140 154 VNHYFQTRHYLHTLW 727 *0701 70 5 ″ ″ 140 154 VNHYFQTRHYLHTLW ″ *1101 76 5 ″ ″ 140 154 VNHYFQTRHYLHTLW ″ *1501 58 5 ″ ″ 141 155 NHYFQTRHYLHTLWK 728 *0701 40 5 ″ ″ 141 155 NHYFQTRHYLHTLWK ″ *1101 79 5 ″ ″ 141 155 NHYFQTRHYLHTLWK ″ *1501 28 5 ″ ″ 142 156 HYFQTRHYLHTLWKA 729 *1101 54 5 ″ ″ 142 156 HYFQTRHYLHTLWKA ″ *1501 30 5 ″ ″ 143 157 YFQTRHYLHTLWKAG 730 *1101 24 5 ″ ″ 144 158 FQTRHYLHTLWKAGI 731 *1101 55 5 ″ ″ 144 158 FQTRHYLHTLWKAGI ″ *1501 5 5 ″ ″ 145 159 QTRHYLHTLWKAGIL 732 *1101 78 5 ″ ″ 145 159 QTRHYLHTLWKAGIL ″ *1501 38 5 ″ ″ 146 160 TRHYLHTLWKAGILY 733 *1101 88 5 ″ ″ 146 160 TRHYLHTLWKAGILY ″ *1501 45 5 ″ ″ 147 161 RHYLHTLWKAGILYK 734 *1101 85 5 ″ ″ 147 161 RHYLHTLWKAGILYK ″ *1501 40 5 ″ ″ 148 162 HYLHTLWKAGILYKR 735 *1101 50 5 ″ ″ 154 168 WKAGILYKRETTRSA 736 *0401 81 5 ″ ″ 155 169 KAGILYKRETTRSAS 737 *0401 83 5 ″ ″ 156 170 AGILYKRETTRSASF 738 *0401 84 5 ″ ″ 157 171 GILYKRETTRSASFC 739 *0401 80 5 ″ ″ 158 172 ILYKRETTRSASFCG 740 *0401 79 5 ″ ″ 159 173 LYKRETTRSASFCGS 741 *0401 14 5 ″ ″ Cumulative Class II-B score: 1519 143 157 YFQTRHYLHTLWKAG 730 *1101 24 6 143 177 144 158 FQTRHYLHTLWKAGI 731 *1101 55 6 ″ ″ 144 158 FQTRHYLHTLWKAGI ″ *1501 5 6 ″ ″ 145 159 QTRHYLHTLWKAGIL 732 *1101 78 6 ″ ″ 145 159 QTRHYLHTLWKAGIL ″ *1501 38 6 ″ ″ 146 160 TRHYLHTLWKAGILY 733 *1101 88 6 ″ ″ 146 160 TRHYLHTLWKAGILY ″ *1501 45 6 ″ ″ 147 161 RHYLHTLWKAGILYK 734 *1101 85 6 ″ ″ 147 161 RHYLHTLWKAGILYK ″ *1501 40 6 ″ ″ 148 162 HYLHTLWKAGILYKR 735 *1101 50 6 ″ ″ 154 168 WKAGILYKRETTRSA 736 *0401 81 6 ″ ″ 155 169 KAGILYKRETTRSAS 737 *0401 83 6 ″ ″ 156 170 AGILYKRETTRSASF 738 *0401 84 6 ″ ″ 157 171 GILYKRETTRSASFC 739 *0401 80 6 ″ ″ 158 172 ILYKRETTRSASFCG 740 *0401 79 6 ″ ″ 159 173 LYKRETTRSASFCGS 741 *0401 14 6 ″ ″ Cumulative Class II-B score: 928 137 151 DQVVNHYFQTRHYLH 724 *0701 53 7 137 170 137 151 DQVVNHYFQTRHYLH ″ *1101 75 7 ″ ″ 137 151 DQVVNHYFQTRHYLH ″ *1501 63 7 ″ ″ 138 152 QVVNHYFQTRHYLHT 725 *0701 63 7 ″ ″ 138 152 QVVNHYFQTRHYLHT ″ *1101 59 7 ″ ″ 138 152 QVVNHYFQTRHYLHT ″ *1501 73 7 ″ ″ 139 153 VVNHYFQTRHYLHTL 726 *0701 88 7 ″ ″ 139 153 VVNHYFQTRHYLHTL ″ *1101 87 7 ″ ″ 139 153 VVNHYFQTRHYLHTL ″ *1501 70 7 ″ ″ 140 154 VNHYFQTRHYLHTLW 727 *0701 70 7 ″ ″ 140 154 VNHYFQTRHYLHTLW ″ *1101 76 7 ″ ″ 140 154 VNHYFQTRHYLHTLW ″ *1501 58 7 ″ ″ 141 155 NHYFQTRHYLHTLWK 728 *0701 40 7 ″ ″ 141 155 NHYFQTRHYLHTLWK ″ *1101 79 7 ″ ″ 141 155 NHYFQTRHYLHTLWK ″ *1501 28 7 ″ ″ 142 156 HYFQTRHYLHTLWKA 729 *1101 54 7 ″ ″ 142 156 HYFQTRHYLHTLWKA ″ *1501 30 7 ″ ″ 143 157 YFQTRHYLHTLWKAG 730 *1101 24 7 ″ ″ 144 158 FQTRHYLHTLWKAGI 731 *1101 55 7 ″ ″ 144 158 FQTRHYLHTLWKAGI ″ *1501 5 7 ″ ″ 145 159 QTRHYLHTLWKAGIL 732 *1101 78 7 ″ ″ 145 159 QTRHYLHTLWKAGIL ″ *1501 38 7 ″ ″ 146 160 TRHYLHTLWKAGILY 733 *1101 88 7 ″ ″ 146 160 TRHYLHTLWKAGILY ″ *1501 45 7 ″ ″ 147 161 RHYLHTLWKAGILYK 734 *1101 85 7 ″ ″ 147 161 RNYLNTLWKAGILYK ″ *1501 40 7 ″ ″ 148 162 HYLHTLWKAGILYKR 735 *1101 50 7 ″ ″ 154 168 WKAGILYKRETTRSA 736 *0401 81 7 ″ ″ 155 169 KAGILYKRETTRSAS 737 *0401 83 7 ″ ″ 156 170 AGILYKRETTRSASF 738 *0401 84 7 ″ ″ Cumulative Class II-B score: 1817 324 338 SCWWLQFRNSKPCSE 742 *0401 3 8 316 347 385 399 TAESRLVVDFSQFSR 743 *0301 97 9 385 417 386 400 AESRLVVDFSQFSRG 744 *0301 87 9 ″ ″ 387 401 ESRLVVDFSQFSRGI 745 *0301 96 9 ″ ″ 388 402 SRLVVDFSQFSRGIS 746 *0301 94 9 ″ ″ 389 403 RLVVDFSQFSRGISR 747 *0301 77 9 ″ ″ 390 404 LVVDFSQFSRGISRV 748 *0301 76 9 ″ ″ Cumulative Class II-B score: 527 421 435 LSSNLSWLSLDVSAA 749 *0401 27 10 419 456 422 436 SSNLSWLSLDVSAAF 750 *0301 57 10 ″ ″ 422 436 SSNLSWLSLDVSAAF ″ *0401 71 10 ″ ″ 423 437 SNLSWLSLDVSAAFY 751 *0301 56 10 ″ ″ 423 437 SNLSWLSLDVSAAFY ″ *0401 70 10 ″ ″ 424 438 NLSWLSLDVSAAFYH 752 *0301 54 10 ″ ″ 424 438 NLSWLSLDVSAAFYN ″ *0401 69 10 ″ ″ 425 439 LSWLSLDVSAAFYNI 753 *0301 53 10 ″ ″ 425 439 LSWLSLDVSAAFYNI ″ *0401 67 10 ″ ″ 425 439 LSWLSLDVSAAFYNI ″ *1301 18 10 ″ ″ 426 440 SWLSLDVSAAFYHIP 754 *0301 51 10 ″ ″ 426 440 SWLSLDVSAAFYHIP ″ *0401 66 10 ″ ″ 427 441 WLSLDVSAAFYNIPL 755 *0301 50 10 ″ ″ 427 441 WLSLDVSAAFYNIPL ″ *0401 17 10 ″ ″ 428 442 LSLDVSAAFYNIPLH 756 *0301 49 10 ″ ″ 432 446 VSAAFYNIPLNPAAM 757 *0101 8 10 ″ ″ 432 446 VSAAFYNIPLNPAAM ″ *0105 8 10 ″ ″ 432 446 VSAAFYNIPLNPAAM ″ *0107 8 10 ″ ″ 433 447 SAAFYNIPLNPAAMP 758 *0101 35 10 ″ ″ 433 447 SAAFYNIPLNPAAMP ″ *0105 35 10 ″ ″ 433 447 SAAFYNIPLNPAAMP ″ *0107 35 10 ″ ″ 433 447 SAAFYNIPLNPAAMP ″ *1101 3 10 ″ ″ 434 448 AAFYNIPLNPAAMPH 759 *0101 13 10 ″ ″ 434 448 AAFYNIPLNPAAMPN ″ *0105 13 10 ″ ″ 434 448 AAFYNIPLNPAAMPN ″ *0107 13 10 ″ ″ Cumulative Class II-B score: 943 422 436 SSNLSWLSLDVSAAF 750 *0301 57 11 422 459 422 436 SSNLSWLSLDVSAAF ″ *0401 71 11 ″ ″ 423 437 SNLSWLSLDVSAAFY 751 *0301 56 11 ″ ″ 423 437 SNLSWLSLDVSAAFY ″ *0401 70 11 ″ ″ 424 438 NLSWLSLDVSAAFYH 752 *0301 54 11 ″ ″ 424 438 NLSWLSLDVSAAFYH ″ *0401 69 11 ″ ″ 425 439 LSWLSLDVSAAFYHI 753 *0301 53 11 ″ ″ 425 439 LSWLSLDVSAAFYHI ″ *0401 67 11 ″ ″ 425 439 LSWLSLDVSAAFYHI ″ *1301 18 11 ″ ″ 426 440 SWLSLDVSAAFYHIP 754 *0301 51 11 ″ ″ 426 440 SWLSLDVSAAFYHIP ″ *0401 66 11 ″ ″ 427 441 WLSLDVSAAFYHIPL 755 *0301 50 11 ″ ″ 427 441 WLSLDVSAAFYHIPL ″ *0401 17 11 ″ ″ 428 442 LSLDVSAAFYHIPLH 756 *0301 49 11 ″ ″ 432 446 VSAAFYHIPLHPAAM 757 *0101 8 11 ″ ″ 432 446 VSAAFYHIPLHPAAM ″ *0105 8 11 ″ ″ 432 446 VSAAFYHIPLHPAAM ″ *0107 8 11 ″ ″ 433 447 SAAFYHIPLHPAAMP 758 *0101 35 11 ″ ″ 433 447 SAAFYHIPLHPAAMP ″ *0105 35 11 ″ ″ 433 447 SAAFYHIPLHPAAMP ″ *0107 35 11 ″ ″ 433 447 SAAFYHIPLHPAAMP ″ *1101 3 11 ″ ″ 434 448 AAFYHIPLHPAAMPH 759 *0101 13 11 ″ ″ 434 448 AAFYHIPLHPAAMPH ″ *0105 13 11 ″ ″ 434 448 AAFYHIPLHPAAMPH ″ *0107 13 11 ″ ″ 444 458 AAMPHLLIGSSGLSR 760 *0101 9 11 ″ ″ 444 458 AAMPHLLIGSSGLSR ″ *0301 64 11 ″ ″ 445 459 AMPHLLIGSSGLSRY 761 *0101 7 11 ″ ″ 445 459 AMPHLLIGSSGLSRY ″ *0301 63 11 ″ ″ Cumulative Class II-B score: 1058 427 441 WLSLDVSAAFYHIPL 755 *0301 50 12 427 459 427 441 WLSLDVSAAFYHIPL ″ *0401 17 12 ″ ″ 428 442 LSLDVSAAFYHIPLH 756 *0301 49 12 ″ ″ 432 446 VSAAFYHIPLHPAAM 757 *0101 8 12 ″ ″ 432 446 VSAAFYHIPLHPAAM ″ *0105 8 12 ″ ″ 432 446 VSAAFYHIPLHPAAM ″ *0107 8 12 ″ ″ 433 447 SAAFYHIPLHPAAMP 758 *0101 35 12 ″ ″ 433 447 SAAFYHIPLHPAAMP ″ *0105 35 12 ″ ″ 433 447 SAAFYHIPLHPAAMP ″ *0107 35 12 ″ ″ 433 447 SAAFYHIPLHPAAMP ″ *1101 3 12 ″ ″ 434 448 AAFYHIPLHPAAMPH 759 *0101 13 12 ″ ″ 434 448 AAFYHIPLHPAAMPH ″ *0105 13 12 ″ ″ 434 448 AAFYHIPLHPAAMPH ″ *0107 13 12 ″ ″ 444 458 AAMPHLLIGSSGLSR 760 *0101 9 12 ″ ″ 444 458 AAMPHLLIGSSGLSR ″ *0301 64 12 ″ ″ 445 459 AMPHLLIGSSGLSRY 761 *0101 7 12 ″ ″ 445 459 AMPHLLIGSSGLSRY ″ *0301 63 12 ″ ″ Cumulative Class II-B score: 426 483 497 SCSRQLYVSLMLLYK 762 *1101 94 13 481 514 484 498 CSRQLYVSLMLLYKT 763 *1101 93 13 ″ ″ 484 498 CSRQLYVSLMLLYKT ″ *1501 20 13 ″ ″ 485 499 SRQLYVSLMLLYKTY 764 *1101 91 13 ″ ″ 485 499 sRQLYVSLMLLYKTY ″ *1501 10 13 ″ ″ 486 500 RQLYVSLMLLYKTYG 765 *0301 47 13 ″ ″ 486 500 RQLYVSLMLLYKTYG ″ *1101 100 13 ″ ″ 486 500 RQLYVSLMLLYKTYG ″ *1301 21 13 ″ ″ 486 500 RQLYVSLMLLYKTYG ″ *1501 23 13 ″ ″ 487 501 QLYVSLMLLYKTYGW 766 *0301 10 13 ″ ″ 487 501 QLYVSLMLLYKTYGW ″ *1101 99 13 ″ ″ 487 501 QLYVSLMLLYKTYGW ″ *1301 20 13 ″ ″ 487 501 QLYVSLMLLYKTYGW ″ *1501 61 13 ″ ″ 488 502 LYVSLMLLYKTYGWK 767 *0301 9 13 ″ ″ 488 502 LYVSLMLLYKTYGWK ″ *1101 97 13 ″ ″ 488 502 LYVSLMLLYKTYGWK ″ *1301 19 13 ″ ″ 488 502 LYVSLMLLYKTYGWK ″ *1501 60 13 ″ ″ 489 503 YVSLMLLYKTYGWKL 768 *0701 100 13 ″ ″ 489 503 YVSLMLLYKTYGWKL ″ *1101 96 13 ″ ″ 489 503 YVSLMLLYKTYGWKL ″ *1301 17 13 ″ ″ 489 503 YVSLMLLYKTYGWKL ″ *1501 99 13 ″ ″ 490 504 VSLMLLYKTYGWKLH 769 *0701 99 13 ″ ″ 490 504 VSLMLLYKTYGWKLH ″ *1301 16 13 ″ ″ 490 504 VSLMLLYKTYGWKLH ″ *1501 100 13 ″ ″ 491 505 SLMLLYKTYGWKLHL 770 *0701 97 13 ″ ″ 491 505 SLMLLYKTYGWKLHL ″ *1301 14 13 ″ ″ 491 505 SLMLLYKTYGWKLHL ″ *1501 97 13 ″ ″ 492 506 LMLLYKTYGWKLHLY 771 *0106 3 13 ″ ″ 492 506 LMLLYKTYGWKLHLY ″ *0701 89 13 ″ ″ 492 506 LMLLYKTYGWKLHLY ″ *1101 5 13 ″ ″ 492 506 LMLLYKTYGWKLHLY ″ *1301 13 13 ″ ″ 492 506 LMLLYKTYGWKLHLY ″ *1501 77 13 ″ ″ 493 507 MLLYKTYGWKLHLYS 772 *0701 87 13 ″ ″ 493 507 MLLYKTYGWKLHLYS ″ *1101 9 13 ″ ″ 493 507 MLLYKTYGWKLHLYS ″ *1501 66 13 ″ ″ 494 508 LLYKTYGWKLHLYSH 773 *0701 84 13 ″ ″ 494 508 LLYKTYGWKLHLYSH ″ *1101 7 13 ″ ″ 494 508 LLYKTYGWKLHLYSH ″ *1501 85 13 ″ ″ 495 509 LYKTYGWKLHLYSHP 774 *0701 74 13 ″ ″ 495 509 LYKTYGWKLHLYSHP ″ *1101 6 13 ″ ″ 495 509 LYKTYGWKLHLYSHP ″ *1501 13 13 ″ ″ 496 510 YKTYGWKLHLYSHPI 775 *1101 4 13 ″ ″ 497 511 KTYGWKLHLYSHPIV 776 *0101 30 13 ″ ″ 497 511 KTYGWKLHLYSHPIV ″ *0701 13 13 ″ ″ 497 511 KTYGWKLHLYSHPIV ″ *1101 3 13 ″ ″ 497 511 KTYGWKLHLYSHPIV ″ *1501 90 13 ″ ″ 498 512 TYGWKLHLYSHPIVL 777 *0101 70 13 ″ ″ 498 512 TYGWKLHLYSHPIVL ″ *0701 71 13 ″ ″ 498 512 TYGWKLHLYSHPIVL ″ *1101 1 13 ″ ″ 498 512 TYGWKLHLYSHPIVL ″ *1501 89 13 ″ ″ 499 513 YGWKLHLYSHPIVLG 778 *0101 81 13 ″ ″ 499 513 YGWKLHLYSHPIVLG ″ *0701 24 13 ″ ″ 499 513 YGWKLHLYSHPIVLG ″ *1301 50 13 ″ ″ 499 513 YGWKLHLYSHPIVLG ″ *1501 87 13 ″ ″ 500 514 GWKLHLYSHPIVLGF 779 *0101 66 13 ″ ″ 500 514 GWKLHLYSHPIVLGF ″ *0701 7 13 ″ ″ 500 514 GWKLHLYSHPIVLGF ″ *1301 49 13 ″ ″ 500 514 GWKLHLYSHPIVLGF ″ *1501 86 13 ″ ″ Cumulative Class II-B score: 3046 524 538 SPFLLAQFTSAICSV 780 *0101 61 14 524 559 524 538 SPFLLAQFTSAICSV ″ *0401 43 14 ″ ″ 524 538 SPFLLAQFTSAICSV ″ *1501 16 14 ″ ″ 525 539 PFLLAQFTSAICSVV 781 *0101 24 14 ″ ″ 525 539 PFLLAQFTSAICSVV ″ *0401 41 14 ″ ″ 525 539 PFLLAQFTSAICSVV ″ *0701 59 14 ″ ″ 525 539 PFLLAQFTSAICSVV ″ *1501 14 14 ″ ″ 526 540 FLLAQFTSAICSVVR 782 *0401 13 14 ″ ″ 526 540 FLLAQFTSAICSVVR ″ *0701 53 14 ″ ″ 527 541 LLAQFTSAICSVVRR 783 *0701 49 14 ″ ″ 528 542 LAQFTSAICSVVRRA 784 *0701 43 14 ″ ″ 529 543 AQFTSAICSVVRRAF 785 *0701 51 14 ″ ″ 533 547 SAICSVVRRAFPHCL 786 *0701 47 14 ″ ″ 533 547 SAICSVVRRAFPHCL ″ *1301 60 14 ″ ″ 534 548 AICSVVRRAFPHCLA 787 *0701 16 14 ″ ″ 534 548 AICSVVRRAFPHCLA ″ *1301 59 14 ″ ″ 535 549 ICSVVRRAFPHCLAF 788 *0106 10 14 ″ ″ 535 549 ICSVVRRAFPHCLAF ″ *0701 21 14 ″ ″ 535 549 ICSVVRRAFPHCLAF ″ *1301 57 14 ″ ″ 536 550 CSVVRRAFPHCLAFS 789 *0103 30 14 ″ ″ 536 550 CSVVRRAFPHCLAFS ″ *0106 30 14 ″ ″ 536 550 CSVVRRAFPHCLAFS ″ *1301 56 14 ″ ″ 537 551 SVVRRAFPHCLAFSY 790 *1301 54 14 ″ ″ 538 552 VVRRAFPHCLAFSYM 791 *1301 53 14 ″ ″ 539 553 VRRAFPHCLAFSYMD 792 *1301 51 14 ″ ″ 545 559 HCLAFSYMDDVVLGA 793 *0401 30 14 ″ ″ Cumulative Class II-B score: 1042 526 540 FLLAQFTSAICSVVR 782 *0401 13 15 526 559 526 540 FLLAQFTSAICSVVR ″ *0701 53 15 ″ ″ 527 541 LLAQFTSAICSVVRR 783 *0701 49 15 ″ ″ 528 542 LAQFTSAICSVVRRA 784 *0701 43 15 ″ ″ 529 543 AQFTSAICSVVRRAF 785 *0701 51 15 ″ ″ 533 547 SAICSVVRRAFPHCL 786 *0701 47 15 ″ ″ 533 547 SAICSVVRRAFPHCL ″ *1301 60 15 ″ ″ 534 548 AICSVVRRAFPHCLA 787 *0701 16 15 ″ ″ 534 548 AICSVVRRAFPHCLA ″ *1301 59 15 ″ ″ 535 549 ICSVVRRAFPHCLAF 788 *0106 10 15 ″ ″ 535 549 ICSVVRRAFPHCLAF ″ *0701 21 15 ″ ″ 535 549 ICSVVRRAFPHCLAF ″ *1301 57 15 ″ ″ 536 550 CSVVRRAFPHCLAFS 789 *0103 30 15 ″ ″ 536 550 CSVVRRAFPHCLAFS ″ *0106 30 15 ″ ″ 536 550 CSVVRRAFPHCLAFS ″ *1301 56 15 ″ ″ 537 551 SVVRRAFPHCLAFSY 790 *1301 54 15 ″ ″ 538 552 VVRRAFPHCLAFSYM 791 *1301 53 15 ″ ″ 539 553 VRRAFPHCLAFSYMD 792 *1301 51 15 ″ ″ 545 559 HCLAFSYMPPVVLGA 793 *0401 30 15 ″ ″ CUMULATIVE CLASS II-B SCORE: 783 565 579 RESLYTAVTNFLLSL 794 *0103 9 16 565 598 565 579 RESLYTAVTNFLLSL ″ *0701 67 16 ″ ″ 566 580 ESLYTAVTNFLLSLG 795 *0701 66 16 ″ ″ 567 581 SLYTAVTNFLLSLGI 796 *0701 64 16 ″ ″ 568 582 LYTAVTNFLLSLGIH 797 *0701 63 16 ″ ″ 569 583 YTAVTNFLLSLGIHL 798 *0101 90 16 ″ ″ 569 583 YTAVTNFLLSLGIHL ″ *0701 61 16 ″ ″ 569 583 YTAVTNFLLSLGIHL ″ *1501 37 16 ″ ″ 570 584 TAVTNFLLSLGIHLN 799 *0101 91 16 ″ ″ 570 584 TAVTNFLLSLGIHLN ″ *0102 28 16 ″ ″ 570 584 TAVTNFLLSLGIHLN ″ *0104 23 16 ″ ″ 570 584 TAVTNFLLSLGIHLN ″ *1501 49 16 ″ ″ 571 585 AVTNFLLSLGIHLNP 800 *0101 89 16 ″ ″ 571 585 AVTNFLLSLGIHLNP ″ *0102 35 16 ″ ″ 571 585 AVTNFLLSLGIHLNP ″ *0104 25 16 ″ ″ 571 585 AVTNFLLSLGIHLNP ″ *1501 46 16 ″ ″ 572 586 VTNFLLSLGIHLNPN 801 *0101 84 16 ″ ″ 572 586 VTNFLLSLGIHLNPN ″ *0102 38 16 ″ ″ 572 586 VTNFLLSLGIHLNPN ″ *0104 38 16 ″ ″ 572 586 VTNFLLSLGIHLNPN ″ *0106 5 16 ″ ″ 572 586 VTNFLLSLGIHLNPN ″ *1501 63 16 ″ ″ 573 587 TNFLLSLGIHLNPNK 802 *0101 83 16 ″ ″ 573 587 TNFLLSLGIHLNPNK ″ *0102 10 16 ″ ″ 573 587 TNFLLSLGIHLNPNK ″ *0104 5 16 ″ ″ 573 587 TNFLLSLGIHLNPNK ″ *0401 4 16 ″ ″ 573 587 TNFLLSLGIHLNPNK ″ *1501 43 16 ″ ″ 574 588 NFLLSLGIHLNPNKT 803 *0101 33 16 ″ ″ 574 588 NFLLSLGIHLNPNKT ″ *1501 30 16 ″ ″ 575 589 FLLSLGIHLNPNKTK 804 *0101 23 16 ″ ″ 575 589 FLLSLGIHLNPNKTK ″ *1501 29 16 ″ ″ 576 590 LLSLGIHLNPNKTKR 805 *1301 25 16 ″ ″ 577 591 LSLGIHLNPNKTKRW 806 *1301 50 16 ″ ″ 578 592 SLGIHLNPNKTKRWG 807 *1301 43 16 ″ ″ 579 593 LGIHLNPNKTKRWGY  808 *1301 36 16 ″ ″ Cumulative Class II-B score: 1482 589 603 KRWGYSLNFMGYIIG 809 *1501 57 17 584 617 590 604 RWGYSLNFMGYIIGS 810 *1501 56 17 ″ ″ 591 605 WGYSLNFMGYIIGSW 811 *1501 34 17 ″ ″ 592 606 GYSLNFMGYIIGSWG 812 *1501 21 17 ″ ″ 593 607 YSLNFMGYIIGSWGT 813 *1501 24 17 ″ ″ 594 608 SLNFMGYIIGSWGTL 814 *1501 11 17 ″ ″ 595 609 LNFMGYIIGSWGTLP 815 *1501 19 17 ″ ″ Cumulative Class II-B score: 223 653 667 YPALMPLYACIQAKQ 816 *1101 11 18 653 691 656 670 LMPLYACIQAKQAFT 817 *0101 58 18 ″ ″ 656 670 LMPLYACIQAKQAFT ″ *0105 58 18 ″ ″ 656 670 LMPLYACIQAKQAFT ″ *0107 58 18 ″ ″ 657 671 MPLYACIQAKQAFTF 818 *0101 75 18 ″ ″ 657 671 MPLYACIQAKQAFTF ″ *0105 75 18 ″ ″ 657 671 MPLYACIQAKQAFTF ″ *0107 75 18 ″ ″ 657 671 MPLYACIQAKQAFTF ″ *1301 41 18 ″ ″ 658 672 PLYACIQAKQAFTFS 819 *0101 48 18 ″ ″ 658 672 PLYACIQAKQAFTFS ″ *0105 48 18 ″ ″ 658 672 PLYACIQAKQAFTFS ″ *0107 48 18 ″ ″ 658 672 PLYACIQAKQAFTFS ″ *1301 40 18 ″ ″ 659 673 LYACIQAKQAFTFSP 820 *1301 39 18 ″ ″ 660 674 YACIQAKQAFTFSPT 821 *1301 37 18 ″ ″ 661 675 ACIQAKQAFTFSPTY 822 *1301 36 18 ″ ″ 662 676 CIQAKQAFTFSPTYK 823 *1301 34 18 ″ ″ 663 677 IQAKQAFTFSPTYKA 824 *0701 6 18 ″ ″ 663 677 IQAKQAFTFSPTYKA ″ *1301 33 18 ″ ″ 664 678 QAKQAFTFSPTYKAF 825 *0401 44 18 ″ ″ 664 678 QAKQAFTFSPTYKAF ″ *0701 37 18 ″ ″ 665 679 AKQAFTFSPTYKAFL 826 *0401 79 18 ″ ″ 665 679 AKQAFTFSPTYKAFL ″ *0701 77 18 ″ ″ 666 680 KQAFTFSPTYKAFLS 827 *0401 33 18 ″ ″ 666 680 KQAFTFSPTYKAFLS ″ *0701 60 18 ″ ″ 666 680 KQAFTFSPTYKAFLS ″ *1101 13 18 ″ ″ 666 680 KQAFTFSPTYKAFLS ″ *1501 8 18 ″ ″ 667 681 QAFTFSPTYKAFLSK 828 *0401 54 18 ″ ″ 667 681 QAFTFSPTYKAFLSK ″ *0701 46 18 ″ ″ 668 682 AFTFSPTYKAFLSKQ 829 *0701 14 18 ″ ″ 669 683 FTFSPTYKAFLSKQY 830 *0701 19 18 ″ ″ 672 686 SPTYKAFLSKQYMNL 831 *1501 3 18 ″ ″ 673 687 PTYKAFLSKQYMNLY 832 *1501 23 18 ″ ″ 677 691 AFLSKQYMNLYPVAR 833 *0101 40 18 ″ ″ Cumulative Class II-B score: 1365 657 671 MPLYACIQAKQAFTF 818 *0101 75 19 657 691 657 671 MPLYACIQAKQAFTF ″ *0105 75 19 ″ ″ 657 671 MPLYACIQAKQAFTF ″ *0107 75 19 ″ ″ 657 671 MPLYACIQAKQAFTF ″ *1301 41 19 ″ ″ 658 672 PLYACIQAKQAFTFS 819 *0101 48 19 ″ ″ 658 672 PLYACIQAKQAFTFS ″ *0105 48 19 ″ ″ 658 672 PLYACIQAKQAFTFS ″ *0107 48 19 ″ ″ 658 672 PLYACIQAKQAFTFS ″ *1301 40 19 ″ ″ 659 673 LYACIQAKQAFTFSP 820 *1301 39 19 ″ ″ 660 674 YACIQAKQAFTFSPT 821 *1301 37 19 ″ ″ 661 675 ACIQAKQAFTFSPTY 822 *1301 36 19 ″ ″ 662 676 CIQAKQAFTFSPTYK 823 *1301 34 19 ″ ″ 663 677 IQAKQAFTFSPTYKA 824 *0701 6 19 ″ ″ 663 677 IQAKQAFTFSPTYKA ″ *1301 33 19 ″ ″ 664 678 QAKQAFTFSPTYKAF 825 *0401 44 19 ″ ″ 664 678 QAKQAFTFSPTYKAF ″ *0701 37 19 ″ ″ 665 679 AKQAFTFSPTYKAFL 826 *0401 79 19 ″ ″ 665 679 AKQAFTFSPTYKAFL ″ *0701 77 19 ″ ″ 666 680 KQAFTFSPTYKAFLS 827 *0401 33 19 ″ ″ 666 680 KQAFTFSPTYKAFLS ″ *0701 60 19 ″ ″ 666 680 KQAFTFSPTYKAFLS ″ *1101 13 19 ″ ″ 666 680 KQAFTFSPTYKAFLS ″ *1501 8 19 ″ ″ 667 681 QAFTFSPTYKAFLSK 828 *0401 54 19 ″ ″ 667 681 QAFTFSPTYKAFLSK ″ *0701 46 19 ″ ″ 668 682 AFTFSPTYKAFLSKQ 829 *0701 14 19 ″ ″ 669 683 FTFSPTYKAFLSKQY 830 *0701 19 19 ″ ″ 672 686 SPTYKAFLSKQYMNL 831 *1501 3 19 ″ ″ 673 687 PTYKAFLSKQYMNLY 832 *1501 23 19 ″ ″ 677 691 AFLSKQYMNLYPVAR 833 *0101 40 19 ″ ″ Cumulative Class II-B score: 1181 717 731 MRGTFVAPLPIHTAE 834 *0101 10 20 715 746 717 731 MRGTFVAPLPIHTAE ″ *0105 10 20 ″ ″ 717 731 MRGTFVAPLPIHTAE ″ *0107 10 20 ″ ″ 718 732 RGTFVAPLPIHTAEL 835 *0101 4 20 ″ ″ 718 732 RGTFVAPLPIHTAEL ″ *0102 20 20 ″ ″ 718 732 RGTFVAPLPIHTAEL ″ *0104 30 20 ″ ″ 718 732 RGTFVAPLPIHTAEL ″ *0105 60 20 ″ ″ 718 732 RGTFVAPLPIHTAEL ″ *0106 33 20 ″ ″ 718 732 RGTFVAPLPIHTAEL ″ *0107 60 20 ″ ″ 719 733 GTFVAPLPIHTAELL 836 *0101 6 20 ″ ″ 732 746 LLAACFARSRSGAKL 837 *0701 1 20 ″ ″ Cumulative Class II-B score: 244 767 781 GCTANWILRGTSFVY 838 *1501 1 21 754 791 768 782 CTANWILRGTSFVYV 839 *1301 21 21 ″ ″ 768 782 CTANWILRGTSFVYV ″ *1501 10 21 ″ ″ 773 787 ILRGTSFVYVPSALN 840 *0101 100 21 ″ ″ 773 787 ILRGTSFVYVPSALN ″ *0401 23 21 ″ ″ 773 787 ILRGTSFVYVPSALN ″ *0701 31 21 ″ ″ 774 788 LRGTSFVYVPSALNP 841 *0101 96 21 ″ ″ 774 788 LRGTSFVYVPSALNP ″ *0105 40 21 ″ ″ 774 788 LRGTSFVYVPSALNP ″ *0107 40 21 ″ ″ 774 788 LRGTSFVYVPSALNP ″ *0401 56 21 ″ ″ 774 788 LRGTSFVYVPSALNP ″ *0701 23 21 ″ ″ 775 789 RGTSFVYVPSALNPA 842 *0101 99 21 ″ ″ 775 789 RGTSFVYVPSALNPA ″ *0102 30 21 ″ ″ 775 789 RGTSFVYVPSALNPA ″ *0104 43 21 ″ ″ 775 789 RGTSFVYVPSALNPA ″ *0105 93 21 ″ ″ 775 789 RGTSFVYVPSALNPA ″ *0107 93 21 ″ ″ 775 789 RGTSFVYVPSALNPA ″ *0401 76 21 ″ ″ 775 789 RGTSFVYVPSALNPA ″ *0701 29 21 ″ ″ 776 790 GTSFVYVPSALNPAD 843 *0101 97 21 ″ ″ 776 790 GTSFVYVPSALNPAD ″ *0102 13 21 ″ ″ 776 790 GTSFVYVPSALNPAD ″ *0104 28 21 ″ ″ 776 790 GTSFVYVPSALNPAD ″ *0105 85 21 ″ ″ 776 790 GTSFVYVPSALNPAD ″ *0107 85 21 ″ ″ 776 790 GTSFVYVPSALNPAD ″ *0401 74 21 ″ ″ 776 790 GTSFVYVPSALNPAD ″ *0701 4 21 ″ ″ 777 791 TSFVYVPSALNPADD 844 *0101 94 21 ″ ″ 777 791 TSFVYVPSALNPADD ″ *0105 68 21 ″ ″ 777 791 TSFVYVPSALNPADD ″ *0107 68 21 ″ ″ 777 791 TSFVYVPSALNPADD ″ *0401 73 21 ″ ″ Cumulative Class II-B score: 1591 767 781 GCTANWILRGTSFVY 838 *1501 1 22 757 792 768 782 CTANWILRGTSFVYV 839 *1301 21 22 ″ ″ 768 782 CTANWILRGTSFVYV ″ *1501 10 22 ″ ″ 773 787 ILRGTSFVYVPSALN 840 *0101 100 22 ″ ″ 773 787 ILRGTSFVYVPSALN ″ *0401 23 22 ″ ″ 773 787 ILRGTSFVYVPSALN ″ *0701 31 22 ″ ″ 774 788 LRGTSFVYVPSALNP 841 *0101 96 22 ″ ″ 774 788 LRGTSFVYVPSALNP ″ *0105 40 22 ″ ″ 774 788 LRGTSFVYVPSALNP ″ *0107 40 22 ″ ″ 774 788 LRGTSFVYVPSALNP ″ *0401 56 22 ″ ″ 774 788 LRGTSFVYVPSALNP ″ *0701 23 22 ″ ″ 775 789 RGTSFVYVPSALNPA 842 *0101 99 22 ″ ″ 775 789 RGTSFVYVPSALNPA ″ *0102 30 22 ″ ″ 775 789 RGTSFVYVPSALNPA ″ *0104 43 22 ″ ″ 775 789 RGTSFVYVPSALNPA ″ *0105 93 22 ″ ″ 775 789 RGTSFVYVPSALNPA ″ *0107 93 22 ″ ″ 775 789 RGTSFVYVPSALNPA ″ *0401 76 22 ″ ″ 775 789 RGTSFVYVPSALNPA ″ *0701 29 22 ″ ″ 776 790 GTSFVYVPSALNPAD 843 *0101 97 22 ″ ″ 776 790 GTSFVYVPSALNPAD ″ *0102 13 22 ″ ″ 776 790 GTSFVYVPSALNPAD ″ *0104 28 22 ″ ″ 776 790 GTSFVYVPSALNPAD ″ *0105 85 22 ″ ″ 776 790 GTSFVYVPSALNPAD ″ *0107 85 22 ″ ″ 776 790 GTSFVYVPSALNPAD ″ *0401 74 22 ″ ″ 776 790 GTSFVYVPSALNPAD ″ *0701 4 22 ″ ″ 777 791 TSFVYVPSALNPADD 844 *0101 94 22 ″ ″ 777 791 TSFVYVPSALNPADD ″ *0105 68 22 ″ ″ 777 791 TSFVYVPSALNPADD ″ *0107 68 22 ″ ″ 777 791 TSFVYVPSALNPADD ″ *0401 73 22 ″ ″ 778 792 SFVYVPSALNPADDP 845 *0101 54 22 ″ ″ 778 792 SFVYVPSALNPADDP ″ *0401 64 22 ″ ″ Cumulative Class II-B score: 1709 767 781 GCTANWILRGTSFVY 838 *1501 1 23 754 789 768 782 CTANWILRGTSFVYV 839 *1301 21 23 ″ ″ 768 782 CTANWILRGTSFVYV ″ *1501 10 23 ″ ″ 773 787 ILRGTSFVYVPSALN 840 *0101 100 23 ″ ″ 773 787 ILRGTSFVYVPSALN ″ *0401 23 23 ″ ″ 773 787 ILRGTSFVYVPSALN ″ *0701 31 23 ″ ″ 774 788 LRGTSFVYVPSALNP 841 *0101 96 23 ″ ″ 774 788 LRGTSFVYVPSALNP ″ *0105 40 23 ″ ″ 774 788 LRGTSFVYVPSALNP ″ *0107 40 23 ″ ″ 774 788 LRGTSFVYVPSALNP ″ *0401 56 23 ″ ″ 774 788 LRGTSFVYVPSALNP ″ *0701 23 23 ″ ″ 775 789 RGTSFVYVPSALNPA 842 *0101 99 23 ″ ″ 775 789 RGTSFVYVPSALNPA ″ *0102 30 23 ″ ″ 775 789 RGTSFVYVPSALNPA ″ *0104 43 23 ″ ″ 775 789 RGTSFVYVPSALNPA ″ *0105 93 23 ″ ″ 775 789 RGTSFVYVPSALNPA ″ *0107 93 23 ″ ″ 775 789 RGTSFVYVPSALNPA ″ *0401 76 23 ″ ″ 775 789 RGTSFVYVPSALNPA ″ *0701 29 23 ″ ″ Cumulative Class II-B score: 903 ″Start″ and ″End″ are relative to the amino acid sequence of human HBV polymerase as depicted in SEQ ID NO: 1 ^(A)Peptide amino acid sequence. Each HLA-DRB1 binding peptide of HBV polymerase is listed separately for each HLA class II molecule to which it is predicted to bind, and each peptide can be listed multiple times for that reason. ^(B)Class II-B score. See Material and Methods (Examples section). ^(C)Cumulative Class II-B score. See Material and Methods (Examples section).

TABLE 5a Predicted HLA class I-restricted CD8⁺ cytotoxic T cell epitopes contained in SLP sequences from HBV Core protein. HLA class I binding peptides in SLP sequences derived from HBV Core protein Peptide of invention SEQ HLA Class Class (SLP) ID class I I-B C- I-BCI SLP SLP Start End Length Sequence^(A) NO: molecule score^(B) score^(C) score^(D) SLP# Start End 107 117 11 DPASRDLVVNY 846 B*3501 100 1,68 168 24 107 141 107 117 11 DPASRDLVVNY ″ B*3503 30 ″ 50 24 ″ ″ 107 117 11 DPASRDLVVNY ″ B*5301 79 ″ 132 24 ″ ″ 108 117 10 PASRDLVVNY 847 B*5701 100 ″ 168 24 ″ ″ 108 117 10 PASRDLVVNY ″ B*5801 100 ″ 168 24 ″ ″ 109 117 9 ASRDLVVNY 848 A*3002 45 ″ 76 24 ″ ″ 109 117 9 ASRDLVVNY ″ B*1501 40 ″ 67 24 ″ ″ 109 117 9 ASRDLVVNY ″ B*1525 10 ″ 17 24 ″ ″ 111 118 8 RDLVVNYV 849 B*1302 63 1,72 108 24 ″ ″ 113 122 10 LVVNYVNTNV 850 A*0206 29 1,04 30 24 ″ ″ 113 122 10 LVVNYVNTNV ″ A*6802 75 ″ 78 24 ″ ″ 114 122 9 VVNYVNTNV 851 A*6802 38 ″ 39 24 ″ ″ 113 123 11 LVVNYVNTNVG 852 A*6802 25 0,09 2 24 ″ ″ 116 124 9 NYVNTNVGL 853 A*2301 63 1,89 118 24 ″ ″ 117 125 9 YVNTNVGLK 854 A*0301 100 0,33 33 24 ″ ″ 117 125 9 YVNTNVGLK ″ A*1101 100 ″ 33 24 ″ ″ 117 125 9 YVNTNVGLK ″ A*6801 62 ″ 20 24 ″ ″ 116 126 11 NYVNTNVGLKI 855 A*2301 44 1,53 67 24 ″ ″ 116 126 11 NYVNTNVGLKI ″ A*2402 63 ″ 96 24 ″ ″ 120 129 10 INVGlKIRQL 856 B*0801 50 1,67 83 24 ″ ″ 121 129 9 NVGLKIRQL 857 B*0702 75 ″ 125 24 ″ ″ 121 130 10 NVGLKIRQLL 858 B*0702 83 1,23 103 24 ″ ″ 123 130 8 GLKIRQLL 859 B*0801 70 ″ 86 24 ″ ″ 122 131 10 VGLKIRQLLW 860 B*5802 55 1,66 91 24 ″ ″ 123 132 10 GLKIRQLLWF 861 A*0301 25 1,02 25 24 ″ ″ 125 132 8 KIRQLLWF 862 A*3201 75 ″ 76 24 ″ ″ 125 132 8 KIRQLLWF ″ B*1501 20 ″ 20 24 ″ ″ 125 132 8 KIRQLLWF ″ B*1525 40 ″ 41 24 ″ ″ 126 134 9 IRQLLWFHI 863 B*2702 86 1,69 145 24 ″ ″ 126 134 9 IRQLLWFHI ″ B*2705 84 ″ 142 24 ″ ″ 127 134 8 RQLLWFHI 864 A*2301 81 ″ 138 24 ″ ″ 127 134 8 RQLLWFHI ″ A*2402 69 ″ 116 24 ″ ″ 127 134 8 RQLLWFHI ″ A*3201 63 ″ 106 24 ″ ″ 127 134 8 RQLLWFHI ″ B*1301 90 ″ 152 24 ″ ″ 127 134 8 RQLLWFHI ″ B*2702 100 ″ 169 24 ″ ″ 127 134 8 RQLLWFHI ″ B*3701 73 ″ 124 24 ″ ″ 127 134 8 RQLLWFHI ″ B*4002 57 ″ 97 24 ″ ″ 127 134 8 RQLLWFHI ″ B*4801 100 ″ 169 24 ″ ″ 127 134 8 RQLLWFHI ″ B*4901 47 ″ 80 24 ″ ″ 127 134 8 RQLLWFHI ″ B*5001 47 ″ 79 24 ″ ″ 127 134 8 RQLLWFHI ″ B*5201 78 ″ 132 24 ″ ″ 126 135 10 IRQLLWFHIS 865 B*2705 3 0,55 2 24 ″ ″ 127 135 9 RQLLWFHIS 866 B*4801 14 ″ 8 24 ″ ″ 127 136 10 RQLLWFHISC 867 B*4801 29 0,82 24 24 ″ ″ 128 136 9 QLLWFHISC 868 A*0201 75 ″ 62 24 ″ ″ 129 136 8 LLWFHISC 869 A*0201 60 ″ 49 24 ″ ″ 127 137 11 RQLLWFHISCL 870 B*1301 35 1,95 68 24 ″ ″ 127 137 11 RQLLWFHISCL ″ B*1302 50 ″ 98 24 ″ ″ 127 137 11 RQLLWFHISCL ″ B*1402 38 ″ 75 24 ″ ″ 127 137 11 RQLLWFHISCL ″ B*2702 71 ″ 139 24 ″ ″ 127 137 11 RQLLWFHISCL ″ B*3701 40 ″ 78 24 ″ ″ 127 137 11 RQLLWFHISCL ″ B*3901 64 ″ 125 24 ″ ″ 127 137 11 RQLLWFHISCL ″ B*4001 7 ″ 13 24 ″ ″ 127 137 11 RQLLWFHISCL ″ B*4002 14 ″ 28 24 ″ ″ 128 137 10 QLLWFHISCL 871 A*0201 20 ″ 39 24 ″ ″ 129 137 9 LLWFHISCL 872 A*0201 50 ″ 98 24 ″ ″ 129 137 9 LLWFHISCL ″ B*0801 50 ″ 98 24 ″ ″ 130 137 8 LWFHISCL 873 A*2301 13 ″ 24 24 ″ ″ 130 137 8 LWFHISCL ″ A*2402 13 ″ 24 24 ″ ″ 129 138 10 LLWFHISCLT 874 A*0201 56 0,32 18 24 ″ ″ 129 139 11 LLWFHISCLTF 875 A*3201 81 1,49 121 24 ″ ″ 129 139 11 LLWFHISCLTF ″ B*1501 100 ″ 149 24 ″ ″ 129 139 11 LLWFHISCLTF ″ B*1502 78 ″ 116 24 ″ ″ 129 139 11 LLWFHISCLTF ″ B*1525 100 ″ 149 24 ″ ″ 130 139 10 LWFHISCLTF 876 A*2301 100 ″ 149 24 ″ ″ 130 139 10 LWFHISCLTF ″ A*2402 100 ″ 149 24 ″ ″ 130 139 10 LWFHISCLTF ″ A*2902 86 ″ 127 24 ″ ″ 130 139 10 LWFHISCLTF ″ B*2702 43 ″ 64 24 ″ ″ 132 139 8 FHISCLTF 877 A*2301 56 ″ 84 24 ″ ″ 132 139 8 FHISCLTF ″ B*1402 54 ″ 80 24 ″ ″ 132 139 8 FHISCLTF ″ B*3503 40 ″ 59 24 ″ ″ 132 139 8 FHISCLTF ″ B*3801 100 ″ 149 24 ″ ″ 132 139 8 FHISCLTF ″ B*3901 57 ″ 85 24 ″ ″ 131 141 11 WFHISCLTFGR 878 A*3101 29 1,41 42 24 ″ ″ 131 141 11 WFHISCLTFGR ″ A*3303 52 ″ 74 24 ″ ″ 132 141 10 FHISCLTFGR 879 A*3101 35 ″ 50 24 ″ ″ 133 141 9 HISCLTFGR 880 A*3101 82 ″ 116 24 ″ ″ 133 141 9 HISCLTFGR ″ A*3303 95 ″ 135 24 ″ ″ 133 141 9 HISCLTFGR ″ A*6801 85 ″ 120 24 ″ ″ 133 141 9 HISCLTFGR ″ A*7401 100 ″ 141 24 ″ ″ 134 141 8 ISCLTFGR 881 A*3101 88 ″ 125 24 ″ ″ 134 141 8 ISCLTFGR ″ A*3303 29 ″ 40 24 ″ ″ 134 141 8 ISCLTFGR ″ A*6801 31 ″ 43 24 ″ ″ 134 141 8 ISCLTFGR ″ A*7401 50 ″ 71 24 ″ ″ Cumulative Class I-BCI 7277 score^(E): 136 145 10 CLTFGRETVL 882 B*0801 100 1,87 187 25 136 169 137 147 11 LTFGRETVLEY 883 A*0101 80 1,68 134 25 ″ ″ 137 147 11 LTFGRETVLEY ″ A*0301 67 ″ 112 25 ″ ″ 137 147 11 LTFGRETVLEY ″ A*2501 80 ″ 134 25 ″ ″ 137 147 11 LTFGRETVLEY ″ A*2601 60 ″ 101 25 ″ ″ 137 147 11 LTFGRETVLEY ″ A*2902 100 ″ 168 25 ″ ″ 137 147 11 LTFGRETVLEY ″ A*3002 100 ″ 168 25 ″ ″ 137 147 11 LTFGRETVLEY ″ B*1501 90 ″ 151 25 ″ ″ 137 147 11 LTFGRETVLEY ″ B*1502 100 ″ 168 25 ″ ″ 137 147 11 LTFGRETVLEY ″ B*4601 67 ″ 112 25 ″ ″ 137 147 11 LTFGRETVLEY ″ B*5701 38 ″ 63 25 ″ ″ 137 147 11 LTFGRETVLEY ″ B*5802 36 ″ 61 25 ″ ″ 139 147 9 FGRETVLEY 884 B*1525 90 ″ 151 25 ″ ″ 139 147 9 FGRETVLEY ″ B*4601 100 ″ 168 25 ″ ″ 138 148 11 TFGRETVLEYL 885 A*2301 6 1,23 8 25 ″ ″ 138 148 11 TFGRETVLEYL ″ A*2402 31 ″ 38 25 ″ ″ 139 148 10 FGRETVLEYL 886 B*0702 100 ″ 123 25 ″ ″ 140 148 9 GRETVLEYL 887 B*2702 21 ″ 26 25 ″ ″ 141 148 8 RETVLEYL 888 B*1301 60 ″ 74 25 ″ ″ 141 148 8 RETVLEYL ″ B*3701 33 ″ 41 25 ″ ″ 141 148 8 RETVLEYL ″ B*4001 100 ″ 123 25 ″ ″ 141 148 8 RETVLEYL ″ B*4002 93 ″ 114 25 ″ ″ 141 148 8 RETVLEYL ″ B*4402 8 ″ 10 25 ″ ″ 141 148 8 RETVLEYL ″ B*4403 54 ″ 66 25 ″ ″ 141 148 8 RETVLEYL ″ B*4801 7 ″ 9 25 ″ ″ 141 148 8 RETVLEYL ″ B*4901 6 ″ 7 25 ″ ″ 139 149 11 FGRETVLEYLV 889 A*0201 45 1,23 55 25 ″ ″ 141 149 9 RETVLEYLV 890 B*1301 30 ″ 37 25 ″ ″ 141 149 9 RETVLEYLV ″ B*1302 38 ″ 46 25 ″ ″ 141 149 9 RETVLEYLV ″ B*3701 27 ″ 33 25 ″ ″ 141 149 9 RETVLEYLV ″ B*4001 67 ″ 82 25 ″ ″ 141 149 9 RETVLEYLV ″ B*4002 79 ″ 96 25 ″ ″ 141 149 9 RETVLEYLV ″ B*4901 71 ″ 87 25 ″ ″ 141 149 9 RETVLEYLV ″ B*5001 27 ″ 33 25 ″ ″ 142 149 8 ETVLEYLV 891 A*2501 20 ″ 25 25 ″ ″ 142 149 8 ETVLEYLV ″ A*2601 50 ″ 61 25 ″ ″ 141 150 10 RETVLEYLVS 892 B*4002 7 0,57 4 25 ″ ″ 141 151 11 RETVLEYLVSF 893 B*1301 45 1,50 67 25 ″ ″ 141 151 11 RETVLEYLVSF ″ B*1801 88 ″ 131 25 ″ ″ 141 151 11 RETVLEYLVSF ″ B*2702 50 ″ 75 25 ″ ″ 141 151 11 RETVLEYLVSF ″ B*4001 80 ″ 120 25 ″ ″ 141 151 11 RETVLEYLVSF ″ B*4002 86 ″ 128 25 ″ ″ 141 151 11 RETVLEYLVSF ″ B*4402 67 ″ 100 25 ″ ″ 141 151 11 RETVLEYLVSF ″ B*4403 77 ″ 115 25 ″ ″ 141 151 11 RETVLEYLVSF ″ B*4901 35 ″ 53 25 ″ ″ 141 151 11 RETVLEYLVSF ″ B*5001 60 ″ 90 25 ″ ″ 142 151 10 ETVLEYLVSF 894 A*2501 100 ″ 150 25 ″ ″ 142 151 10 ETVLEYLVSF ″ A*2601 100 ″ 150 25 ″ ″ 143 151 9 TVLEYLVSF 895 A*3201 50 ″ 75 25 ″ ″ 143 151 9 TVLEYLVSF ″ B*1525 20 ″ 30 25 ″ ″ 145 152 8 LEYLVSFG 896 B*4901 18 0,48 8 25 ″ ″ 143 153 11 TVLEYLVSFGV 897 A*0201 90 1,80 162 25 ″ ″ 143 153 11 TVLEYLVSFGV ″ A*6802 100 ″ 180 25 ″ ″ 144 153 10 VLEYLVSFGV 898 A*0201 65 ″ 117 25 ″ ″ 145 153 9 LEYLVSFGV 899 A*0201 67 ″ 120 25 ″ ″ 145 153 9 LEYLVSFGV ″ B*1301 75 ″ 135 25 ″ ″ 145 153 9 LEYLVSFGV ″ B*1801 63 ″ 113 25 ″ ″ 145 153 9 LEYLVSFGV ″ B*3701 67 ″ 120 25 ″ ″ 145 153 9 LEYLVSFGV ″ B*4001 73 ″ 132 25 ″ ″ 145 153 9 LEYLVSFGV ″ B*4002 29 ″ 51 25 ″ ″ 145 153 9 LEYLVSFGV ″ B*4402 42 ″ 75 25 ″ ″ 145 153 9 LEYLVSFGV ″ B*4901 94 ″ 170 25 ″ ″ 145 153 9 LEYLVSFGV ″ B*5001 87 ″ 156 25 ″ ″ 145 153 9 LEYLVSFGV ″ B*5201 56 ″ 100 25 ″ ″ 145 154 10 LEYLVSFGVW 900 B*1301 65 1,34 87 25 ″ ″ 145 154 10 LEYLVSFGVW ″ B*1302 13 ″ 17 25 ″ ″ 145 154 10 LEYLVSFGVW ″ B*3801 11 ″ 15 25 ″ ″ 145 154 10 LEYLVSFGVW ″ B*4402 92 ″ 123 25 ″ ″ 145 154 10 LEYLVSFGVW ″ B*4403 92 ″ 124 25 ″ ″ 145 154 10 LEYLVSFGVW ″ B*4901 88 ″ 118 25 ″ ″ 145 154 10 LEYLVSFGVW ″ B*5201 22 ″ 30 25 ″ ″ 146 154 9 EYLVSFGVW 901 A*2301 69 ″ 92 25 ″ ″ 146 154 9 EYLVSFGVW ″ A*2402 81 ″ 109 25 ″ ″ 147 154 8 YLVSFGVW 902 B*5701 13 ″ 17 25 ″ ″ 147 154 8 YLVSFGVW ″ B*5801 36 ″ 48 25 ″ ″ 145 155 11 LEYLVSFGVWI 903 B*1301 85 1,63 139 25 ″ ″ 145 155 11 LEYLVSFGVWI ″ B*1302 88 ″ 143 25 ″ ″ 145 155 11 LEYLVSFGVWI ″ B*1801 50 ″ 82 25 ″ ″ 145 155 11 LEYLVSFGVWI ″ B*3701 80 ″ 130 25 ″ ″ 145 155 11 LEYLVSFGVWI ″ B*3801 78 ″ 127 25 ″ ″ 145 155 11 LEYLVSFGVWI ″ B*4001 60 ″ 98 25 ″ ″ 145 155 11 LEYLVSFGVWI ″ B*4002 43 ″ 70 25 ″ ″ 145 155 11 LEYLVSFGVWI ″ B*4402 50 ″ 82 25 ″ ″ 145 155 11 LEYLVSFGVWI ″ B*4403 62 ″ 100 25 ″ ″ 145 155 11 LEYLVSFGVWI ″ B*4901 100 ″ 163 25 ″ ″ 145 155 11 LEYLVSFGVWI ″ B*5001 80 ″ 130 25 ″ ″ 145 155 11 LEYLVSFGVWI ″ B*5201 89 ″ 145 25 ″ ″ 147 155 9 YLVSFGVWI 904 A*0201 75 ″ 122 25 ″ ″ 146 156 11 EYLVSFGVWIR 905 A*3303 71 1,61 115 25 ″ ″ 147 156 10 YLVSFGVWIR 906 A*0301 100 ″ 161 25 ″ ″ 147 156 10 YLVSFGVWIR ″ A*6801 54 ″ 87 25 ″ ″ 148 156 9 LVSFGVWIR 907 A*3101 12 ″ 19 25 ″ ″ 148 156 9 LVSFGVWIR ″ A*3303 38 ″ 61 25 ″ ″ 148 156 9 LVSFGVWIR ″ A*6801 23 ″ 37 25 ″ ″ 148 156 9 LVSFGVWIR ″ A*7401 40 ″ 64 25 ″ ″ 149 156 8 VSFGVWIR 908 A*1101 13 ″ 20 25 ″ ″ 149 156 8 VSFGVWIR ″ A*3101 59 ″ 95 25 ″ ″ 149 156 8 VSFGVWIR ″ A*3303 48 ″ 77 25 ″ ″ 149 156 8 VSFGVWIR ″ A*6801 77 ″ 124 25 ″ ″ 149 156 8 VSFGVWIR ″ A*7401 80 ″ 129 25 ″ ″ 148 157 10 LVSFGVWIRT 909 A*3201 88 0,42 37 25 ″ ″ 148 158 11 LVSFGVWIRTP 910 A*6802 63 0,28 17 25 ″ ″ 151 160 10 FGVWIRTPPA 911 B*5501 55 0,99 54 25 ″ ″ 151 160 10 FGVWIRTPPA ″ B*5601 64 ″ 63 25 ″ ″ 151 161 11 FGVWIRTPPAY 912 A*2902 57 1,46 83 25 ″ ″ 151 161 11 FGVWIRTPPAY ″ B*1502 56 ″ 81 25 ″ ″ 151 161 11 FGVWIRTPPAY ″ B*3501 89 ″ 130 25 ″ ″ 151 161 11 FGVWIRTPPAY ″ B*4601 33 ″ 49 25 ″ ″ 152 161 10 GVWIRTPPAY 913 A*3001 67 ″ 97 25 ″ ″ 152 161 10 GVWIRTPPAY ″ B*1502 22 ″ 32 25 ″ ″ 153 161 9 VWIRTPPAY 914 A*2902 79 ″ 114 25 ″ ″ 153 161 9 VWIRTPPAY ″ A*3002 91 ″ 132 25 ″ ″ 154 161 8 WIRTPPAY 915 A*2601 30 ″ 44 25 ″ ″ 154 161 8 WIRTPPAY ″ A*2902 14 ″ 21 25 ″ ″ 154 161 8 WIRTPPAY ″ B*1501 70 ″ 102 25 ″ ″ 154 161 8 WIRTPPAY ″ B*1502 89 ″ 130 25 ″ ″ 154 161 8 WIRTPPAY ″ B*1525 50 ″ 73 25 ″ ″ 152 162 11 GVWIRTPPAYR 916 A*0301 33 0,95 32 25 ″ ″ 152 162 11 GVWIRTPPAYR ″ A*1101 38 ″ 36 25 ″ ″ 152 162 11 GVWIRTPPAYR ″ A*3101 100 ″ 95 25 ″ ″ 152 162 11 GVWIRTPPAYR ″ A*3303 76 ″ 72 25 ″ ″ 152 162 11 GVWIRTPPAYR ″ A*7401 90 ″ 86 25 ″ ″ 153 162 10 VWIRTPPAYR 917 A*3101 6 ″ 6 25 ″ ″ 153 162 10 VWIRTPPAYR ″ A*3303 33 ″ 32 25 ″ ″ 154 162 9 WIRTPPAYR 918 A*3303 90 ″ 86 25 ″ ″ 154 162 9 WIRTPPAYR ″ A*7401 70 ″ 67 25 ″ ″ 156 165 10 RTPPAYRPPN 919 A*3001 83 0,09 7 25 ″ ″ 158 168 11 PPAYRPPNAPI 920 B*0702 17 1,00 17 25 ″ ″ 160 168 9 AYRPPNAPI 921 A*2402 25 ″ 25 25 ″ ″ 160 168 9 AYRPPNAPI ″ A*3001 42 ″ 41 25 ″ ″ 160 169 10 AYRPPNAPIL 922 A*2402 6 1,90 12 25 ″ ″ 160 169 10 AYRPPNAPIL ″ B*0702 50 ″ 95 25 ″ ″ 161 169 9 YRPPNAPIL 923 B*3901 36 ″ 68 25 ″ ″ Cumulative BCI Class I- 11331  score: ″Start″ and ″End″ are relative to the amino acid sequence of HBV core protein as depicted in SEQ ID NO: 4 ^(A)Peptide amino acid sequence. Each HLA class I binding peptide of HBV core protein is listed separately for each HLA class I molecule to which it is predicted to bind, and can be listed multiple times for that reason. ^(B)Class I-B score. See Material and Methods of Examples section. ^(C)C-score. See Material and Methods of Examples section. ^(D)Class I-BCI score. See Material and Methods (Examples section). ^(E)Cumulative Class I-BCI score. See Material and Methods (Examples section).

TABLE 5b Predicted HLA class II-restricted CD4⁺ T cell epitopes contained in SLP sequences from HBV Core protein. HLA class II binding peptides in SLP sequences derived from HBV Core protein Peptide of invention HLA- Class (SLP) SEQ ID DRB1 II-B SLP SLP Start End Sequence^(A) NO: molecule score^(B) SLP# Start End 107 121 DPASRDLVVNYVNTN 924 *0301 46 24 107 141 108 122 PASRDLVVNYVNTNV 925 *0401 69 24 ″ ″ 108 122 PASRDLVVNYVNTNV ″ *1301 10 24 ″ ″ 109 123 ASRDLVVNYVNTNVG 926 *0401 85 24 ″ ″ 109 123 ASRDLVVNYVNTNVG ″ *1301 20 24 ″ ″ 110 124 SRDLVVNYVNTNVGL 927 *0401 92 24 ″ ″ 110 124 SRDLVVNYVNTNVGL ″ *1301 40 24 ″ ″ 111 125 RDLVVNYVNTNVGLK 928 *0103 17 24 ″ ″ 111 125 RDLVVNYVNTNVGLK ″ *0401 100 24 ″ ″ 111 125 RDLVVNYVNTNVGLK ″ *1301 50 24 ″ ″ 112 126 DLVVNYVNTNVGLKI 929 *0103 50 24 ″ ″ 112 126 DLVVNYVNTNVGLKI ″ *0106 25 24 ″ ″ 112 126 DLVVNYVNTNVGLKI ″ *0301 62 24 ″ ″ 112 126 DLVVNYVNTNVGLKI ″ *0401 77 24 ″ ″ 112 126 DLVVNYVNTNVGLKI ″ *0701 15 24 ″ ″ 112 126 DLVVNYVNTNVGLKI ″ *1301 80 24 ″ ″ 113 127 LVVNYVNTNVGLKIR 930 *0103 100 24 ″ ″ 113 127 LVVNYVNTNVGLKIR ″ *0104 35 24 ″ ″ 113 127 LVVNYVNTNVGLKIR ″ *0106 75 24 ″ ″ 113 127 LVVNYVNTNVGLKIR ″ *0301 69 24 ″ ″ 113 127 LVVNYVNTNVGLKIR ″ *0701 50 24 ″ ″ 113 127 LVVNYVNTNVGLKIR ″ *1301 100 24 ″ ″ 114 128 VVNYVNTNVGLKIRQ 931 *0103 83 24 ″ ″ 114 128 VVNYVNTNVGLKIRQ ″ *0104 45 24 ″ ″ 114 128 VVNYVNTNVGLKIRQ ″ *0106 80 24 ″ ″ 114 128 VVNYVNTNVGLKIRQ ″ *1301 90 24 ″ ″ 115 129 VNYVNTNVGLKIRQL 932 *0101 21 24 ″ ″ 115 129 VNYVNTNVGLKIRQL ″ *0102 10 24 ″ ″ 115 129 VNYVNTNVGLKIRQL ″ *0103 67 24 ″ ″ 115 129 VNYVNTNVGLKIRQL ″ *0104 65 24 ″ ″ 115 129 VNYVNTNVGLKIRQL ″ *0105 19 24 ″ ″ 115 129 VNYVNTNVGLKIRQL ″ *0106 85 24 ″ ″ 115 129 VNYVNTNVGLKIRQL ″ *0107 21 24 ″ ″ 115 129 VNYVNTNVGLKIRQL ″ *0701 33 24 ″ ″ 115 129 VNYVNTNVGLKIRQL ″ *1301 70 24 ″ ″ 116 130 NYVNTNVGLKIRQLL 933 *0103 33 24 ″ ″ 116 130 NYVNTNVGLKIRQLL ″ *0104 25 24 ″ ″ 116 130 NYVNTNVGLKIRQLL ″ *0106 65 24 ″ ″ 116 130 NYVNTNVGLKIRQLL ″ *1301 60 24 ″ ″ 117 131 YVNTNVGLKIRQLLW 934 *1101 54 24 ″ ″ 117 131 YVNTNVGLKIRQLLW ″ *1301 30 24 ″ ″ 118 132 VNTNVGLKIRQLLWF 935 *0301 38 24 ″ ″ 118 132 VNTNVGLKIRQLLWF ″ *1301 46 24 ″ ″ 119 133 NTNVGLKIRQLLWFH 936 *0301 31 24 ″ ″ 119 133 NTNVGLKIRQLLWFH ″ *1301 38 24 ″ ″ 120 134 TNVGLKIRQLLWFHI 937 *0102 70 24 ″ ″ 120 134 TNVGLKIRQLLWFHI ″ *0104 55 24 ″ ″ 120 134 TNVGLKIRQLLWFHI ″ *0106 40 24 ″ ″ 120 134 TNVGLKIRQLLWFHI ″ *0301 23 24 ″ ″ 120 134 TNVGLKIRQLLWFHI ″ *0701 38 24 ″ ″ 120 134 TNVGLKIRQLLWFHI ″ *1301 31 24 ″ ″ 120 134 TNVGLKIRQLLWFHI ″ *1501 38 24 ″ ″ 121 135 NVGLKIRQLLWFHIS 938 *0101 11 24 ″ ″ 121 135 NVGLKIRQLLWFHIS ″ *0102 85 24 ″ ″ 121 135 NVGLKIRQLLWFHIS ″ *0104 75 24 ″ ″ 121 135 NVGLKIRQLLWFHIS ″ *0105 10 24 ″ ″ 121 135 NVGLKIRQLLWFHIS ″ *0106 50 24 ″ ″ 121 135 NVGLKIRQLLWFHIS ″ *0107 11 24 ″ ″ 121 135 NVGLKIRQLLWFHIS ″ *0301 15 24 ″ ″ 121 135 NVGLKIRQLLWFHIS ″ *0701 23 24 ″ ″ 121 135 NVGLKIRQLLWFHIS ″ *1301 23 24 ″ ″ 121 135 NVGLKIRQLLWFHIS ″ *1501 85 24 ″ ″ 122 136 VGLKIRQLLWFHISC 939 *0102 65 24 ″ ″ 122 136 VGLKIRQLLWFHISC ″ *0104 50 24 ″ ″ 122 136 VGLKIRQLLWFHISC ″ *0106 20 24 ″ ″ 122 136 VGLKIRQLLWFHISC ″ *0301 8 24 ″ ″ 122 136 VGLKIRQLLWFHISC ″ *1301 15 24 ″ ″ 122 136 VGLKIRQLLWFHISC ″ *1501 46 24 ″ ″ 123 137 GLKIRQLLWFHISCL 940 *0101 31 24 ″ ″ 123 137 GLKIRQLLWFHISCL ″ *0102 75 24 ″ ″ 123 137 GLKIRQLLWFHISCL ″ *0104 80 24 ″ ″ 123 137 GLKIRQLLWFHISCL ″ *0106 55 24 ″ ″ 123 137 GLKIRQLLWFHISCL ″ *0701 100 24 ″ ″ 123 137 GLKIRQLLWFHISCL ″ *1301 8 24 ″ ″ 123 137 GLKIRQLLWFHISCL ″ *1501 100 24 ″ ″ 124 138 LKIRQLLWFHISCLT 941 *0101 26 24 ″ ″ 124 138 LKIRQLLWFHISCLT ″ *0102 80 24 ″ ″ 124 138 LKIRQLLWFHISCLT ″ *0104 70 24 ″ ″ 124 138 LKIRQLLWFHISCLT ″ *0105 24 24 ″ ″ 124 138 LKIRQLLWFHISCLT ″ *0106 60 24 ″ ″ 124 138 LKIRQLLWFHISCLT ″ *0107 26 24 ″ ″ 124 138 LKIRQLLWFHISCLT ″ *0701 92 24 ″ ″ 124 138 LKIRQLLWFHISCLT ″ *1501 92 24 ″ ″ 125 139 KIRQLLWFHISCLTF 942 *0101 5 24 ″ ″ 125 139 KIRQLLWFHISCLTF ″ *0102 50 24 ″ ″ 125 139 KIRQLLWFHISCLTF ″ *0104 40 24 ″ ″ 125 139 KIRQLLWFHISCLTF ″ *0105 5 24 ″ ″ 125 139 KIRQLLWFHISCLTF ″ *0106 35 24 ″ ″ 125 139 KIRQLLWFHISCLTF ″ *0107 5 24 ″ ″ 125 139 KIRQLLWFHISCLTF ″ *0701 85 24 ″ ″ 125 139 KIRQLLWFHISCLTF ″ *1501 31 24 ″ ″ 126 140 IRQLLWFHISCLTFG 943 *0102 40 24 ″ ″ 126 140 IRQLLWFHISCLTFG ″ *0701 46 24 ″ ″ 126 140 IRQLLWFHISCLTFG ″ *1101 69 24 ″ ″ 127 141 RQLLWFHISCLTFGR 944 *0701 8 24 ″ ″ 127 141 RQLLWFHISCLTFGR ″ *1101 46 24 ″ ″ Cumulative Class II-B score^(C): 4649 139 153 FGRETVLEYLVSFGV 945 *0101 42 25 136 169 139 153 FGRETVLEYLVSFGV ″ *0102 35 25 ″ ″ 139 153 FGRETVLEYLVSFGV ″ *0105 38 25 ″ ″ 139 153 FGRETVLEYLVSFGV ″ *0107 42 25 ″ ″ 139 153 FGRETVLEYLVSFGV ″ *0701 69 25 ″ ″ 139 153 FGRETVLEYLVSFGV ″ *1501 23 25 ″ ″ 140 154 GRETVLEYLVSFGVW 946 *0101 46 25 ″ ″ 140 154 GRETVLEYLVSFGVW ″ *0102 55 25 ″ ″ 140 154 GRETVLEYLVSFGVW ″ *0104 60 25 ″ ″ 140 154 GRETVLEYLVSFGVW ″ *0105 67 25 ″ ″ 140 154 GRETVLEYLVSFGVW ″ *0106 45 25 ″ ″ 140 154 GRETVLEYLVSFGVW ″ *0107 74 25 ″ ″ 140 154 GRETVLEYLVSFGVW ″ *0701 62 25 ″ ″ 140 154 GRETVLEYLVSFGVW ″ *1501 15 25 ″ ″ 141 155 RETVLEYLVSFGVWI 947 *0101 92 25 ″ ″ 141 155 RETVLEYLVSFGVWI ″ *0102 95 25 ″ ″ 141 155 RETVLEYLVSFGVWI ″ *0104 90 25 ″ ″ 141 155 RETVLEYLVSFGVWI ″ *0105 81 25 ″ ″ 141 155 RETVLEYLVSFGVWI ″ *0106 90 25 ″ ″ 141 155 RETVLEYLVSFGVWI ″ *0107 89 25 ″ ″ 141 155 RETVLEYLVSFGVWI ″ *0701 77 25 ″ ″ 141 155 RETVLEYLVSFGVWI ″ *1501 8 25 ″ ″ 142 156 ETVLEYLVSFGVWIR 948 *0101 100 25 ″ ″ 142 156 ETVLEYLVSFGVWIR ″ *0102 100 25 ″ ″ 142 156 ETVLEYLVSFGVWIR ″ *0104 100 25 ″ ″ 142 156 ETVLEYLVSFGVWIR ″ *0105 90 25 ″ ″ 142 156 ETVLEYLVSFGVWIR ″ *0106 100 25 ″ ″ 142 156 ETVLEYLVSFGVWIR ″ *0107 100 25 ″ ″ 142 156 ETVLEYLVSFGVWIR ″ *0701 54 25 ″ ″ 142 156 ETVLEYLVSFGVWIR ″ *1301 100 25 ″ ″ 142 156 ETVLEYLVSFGVWIR ″ *1501 77 25 ″ ″ 143 157 TVLEYLVSFGVWIRT 949 *0101 85 25 ″ ″ 143 157 TVLEYLVSFGVWIRT ″ *0102 90 25 ″ ″ 143 157 TVLEYLVSFGVWIRT ″ *0104 95 25 ″ ″ 143 157 TVLEYLVSFGVWIRT ″ *0105 86 25 ″ ″ 143 157 TVLEYLVSFGVWIRT ″ *0106 95 25 ″ ″ 143 157 TVLEYLVSFGVWIRT ″ *0107 95 25 ″ ″ 143 157 TVLEYLVSFGVWIRT ″ *0701 31 25 ″ ″ 143 157 TVLEYLVSFGVWIRT ″ *1301 92 25 ″ ″ 143 157 TVLEYLVSFGVWIRT ″ *1501 69 25 ″ ″ 144 158 VLEYLVSFGVWIRTP 950 *0101 69 25 ″ ″ 144 158 VLEYLVSFGVWIRTP ″ *0102 60 25 ″ ″ 144 158 VLEYLVSFGVWIRTP ″ *0104 85 25 ″ ″ 144 158 VLEYLVSFGVWIRTP ″ *0105 76 25 ″ ″ 144 158 VLEYLVSFGVWIRTP ″ *0106 70 25 ″ ″ 144 158 VLEYLVSFGVWIRTP ″ *0107 84 25 ″ ″ 144 158 VLEYLVSFGVWIRTP ″ *1301 85 25 ″ ″ 144 158 VLEYLVSFGVWIRTP ″ *1501 62 25 ″ ″ 145 159 LEYLVSFGVWIRTPP 951 *0101 62 25 ″ ″ 145 159 LEYLVSFGVWIRTPP ″ *0102 15 25 ″ ″ 145 159 LEYLVSFGVWIRTPP ″ *0104 20 25 ″ ″ 145 159 LEYLVSFGVWIRTPP ″ *0105 48 25 ″ ″ 145 159 LEYLVSFGVWIRTPP ″ *0107 53 25 ″ ″ 145 159 LEYLVSFGVWIRTPP ″ *1301 77 25 ″ ″ 145 159 LEYLVSFGVWIRTPP ″ *1501 54 25 ″ ″ 146 160 EYLVSFGVWIRTPPA 952 *1301 69 25 ″ ″ 147 161 YLVSFGVWIRTPPAY 953 *1301 62 25 ″ ″ 148 162 LVSFGVWIRTPPAYR 954 *0101 32 25 ″ ″ 148 162 LVSFGVWIRTPPAYR ″ *0105 29 25 ″ ″ 148 162 LVSFGVWIRTPPAYR ″ *0107 32 25 ″ ″ 148 162 LVSFGVWIRTPPAYR ″ *0401 40 25 ″ ″ 148 162 LVSFGVWIRTPPAYR ″ *1301 54 25 ″ ″ 149 163 VSFGVWIRTPPAYRP 955 *0101 63 25 ″ ″ 149 163 VSFGVWIRTPPAYRP ″ *0102 25 25 ″ ″ 149 163 VSFGVWIRTPPAYRP ″ *0105 57 25 ″ ″ 149 163 VSFGVWIRTPPAYRP ″ *0107 63 25 ″ ″ 149 163 VSFGVWIRTPPAYRP ″ *0401 60 25 ″ ″ 149 163 VSFGVWIRTPPAYRP ″ *1101 25 25 ″ ″ 150 164 SFGVWIRTPPAYRPP 956 *0101 68 25 ″ ″ 150 164 SFGVWIRTPPAYRPP ″ *0102 30 25 ″ ″ 150 164 SFGVWIRTPPAYRPP ″ *0105 62 25 ″ ″ 150 164 SFGVWIRTPPAYRPP ″ *0107 68 25 ″ ″ 150 164 SFGVWIRTPPAYRPP ″ *0401 80 25 ″ ″ 150 164 SFGVWIRTPPAYRPP ″ *1101 75 25 ″ ″ 151 165 FGVWIRTPPAYRPPN 957 *0101 79 25 ″ ″ 151 165 FGVWIRTPPAYRPPN ″ *0102 45 25 ″ ″ 151 165 FGVWIRTPPAYRPPN ″ *0104 30 25 ″ ″ 151 165 FGVWIRTPPAYRPPN ″ *0105 71 25 ″ ″ 151 165 FGVWIRTPPAYRPPN ″ *0106 5 25 ″ ″ 151 165 FGVWIRTPPAYRPPN ″ *0107 79 25 ″ ″ 151 165 FGVWIRTPPAYRPPN ″ *0401 100 25 ″ ″ 151 165 FGVWIRTPPAYRPPN ″ *1101 100 25 ″ ″ 152 166 GVWIRTPPAYRPPNA 958 *0101 58 25 ″ ″ 152 166 GVWIRTPPAYRPPNA ″ *0105 52 25 ″ ″ 152 166 GVWIRTPPAYRPPNA ″ *0107 58 25 ″ ″ 152 166 GVWIRTPPAYRPPNA ″ *1101 50 25 ″ ″ Cumulative Class II-B score: 5493 ″Start″ and ″End″ are relative to the amino acid sequence of human HBV core protein as depicted in SEQ ID NO: 4 APeptide amino acid sequence. Each HLA-DRB1 binding peptide of HBV core is listed separately for each HLA class II molecule to which it is predicted to bind, and each peptide can be listed multiple times for that reason. ^(B)Class II-B score. See Material and Methods (Examples section). ^(C)Cumulative Class II-B score. See Material and Methods (Examples section).

TABLE 6a Predicted HLA class I-restricted CD8⁺ cytotoxic T cell epitopes contained in SLP sequences from HBV X protein (consensus sequence). HLA class I binding peptides in SLP sequences derived from HBV X protein (consensus sequence) Peptide of HLS ClassI- Class I- invention (SLP) SEQ class I B BCI SLP SLP Start End Length Sequence^(A) ID NO: molecule score^(B) C-score^(C) score^(D) SLP# End Start 36 44 9 ALPSPSPSA  959 A*0201 20 0,97 19 26  36  68 37 44 8 LPSPSPSA  960 B*3501 92 89 26 ″ ″ 37 44 8 LPSPSPSA ″ B*5101 82 ″ 79 26 ″ ″ 37 44 8 LPSPSPSA ″ B*5501 63 ″ 61 26 ″ ″ 37 44 8 LPSPSPSA ″ B*5601 92 ″ 89 26 ″ ″ 36 45 10 ALPSPSPSAV  961 A*0201 90 1,49 134 26 ″ ″ 37 45 9 LPSPSPSAV  962 B*3503 75 ″ 112 26 ″ ″ 37 45 9 LPSPSPSAV ″ B*5101 100 ″ 149 26 ″ ″ 37 45 9 LPSPSPSAV ″ B*5501 94 ″ 139 26 ″ ″ 37 45 9 LPSPSPSAV ″ B*5601 46 ″ 69 26 ″ ″ 37 45 9 LPSPSPSAV ″ B*0701 50 ″ 74 26 ″ ″ 37 47 11 LPSPSPSAVPA  963 A*6802 20 1,05 21 26 ″ ″ 37 47 11 LPSPSPSAVPA ″ B*3501 33 ″ 35 26 ″ ″ 37 47 11 LPSPSPSAVPA ″ B*3503 58 ″ 61 26 ″ ″ 37 47 11 LPSPSPSAVPA ″ B*5101 55 ″ 57 26 ″ ″ 37 47 11 LPSPSPSAVPA ″ B*5501 88 ″ 92 26 ″ ″ 37 47 11 LPSPSPSAVPA ″ B*5601 77 ″ 81 26 ″ ″ 37 47 11 LPSPSPSAVPA ″ B*0701 25 ″ 26 26 ″ ″ 39 47 9 SPSPSAVPA  964 B*5501 56 ″ 59 26 ″ ″ 39 47 9 SPSPSAVPA ″ B*5601 85 ″ 89 26 ″ ″ 41 51 11 SPSAVPADHGA  965 B*5501 6 1,30 8 26 ″ ″ 41 51 11 SPSAVPADHGA ″ B*5601 8 ″ 10 26 ″ ″ 44 53 10 AVPADHGAHL  966 B*0701 75 1,87 140 26 ″ ″ 45 53 9 VPADHGAHL  967 B*1402 43 ″ 80 26 ″ ″ 45 53 9 VPADHGAHL ″ B*3503 42 ″ 78 26 ″ ″ 45 53 9 VPADHGAHL ″ B*5501 31 ″ 59 26 ″ ″ 45 53 9 VPADHGAHL ″ B*0701 100 ″ 187 26 ″ ″ 45 55 11 VPADHGAHLSL  968 B*1402 93 1,93 180 26 ″ ″ 45 55 11 VPADHGAHLSL ″ B*3501 67 ″ 129 26 ″ ″ 45 55 11 VPADHGAHLSL ″ B*3503 100 ″ 193 26 ″ ″ 45 55 11 VPADHGAHLSL ″ B*5101 73 ″ 141 26 ″ ″ 45 55 11 VPADHGAHLSL ″ B*5301 29 ″ 55 26 ″ ″ 45 55 11 VPADHGAHLSL ″ B*5501 50 ″ 97 26 ″ ″ 45 55 11 VPADHGAHLSL ″ B*0701 100 ″ 193 26 ″ ″ 47 55 9 ADHGAHLSL  969 B*4002 14 ″ 28 26 ″ ″ 48 55 8 DHGAHLSL  970 B*1402 79 ″ 152 26 ″ ″ 49 56 8 HGAHLSLR  971 A*3303 73 0,63 46 26 ″ ″ 49 56 8 HGAHLSLR ″ A*6801 33 ″ 21 26 ″ ″ 50 58 9 GAHLSLRGL  972 B*0701 25 1,33 33 26 ″ ″ 51 58 8 AHLSLRGL  973 B*1402 29 ″ 38 26 ″ ″ 51 58 8 AHLSLRGL ″ B*3901 9 ″ 12 26 ″ ″ 51 60 10 AHLSLRGLPV  974 B*1402 71 1,05 75 26 ″ ″ 51 60 10 AHLSLRGLPV ″ B*3901 36 ″ 38 26 ″ ″ 52 60 9 HLSLRGLPV  975 B*0801 40 ″ 42 26 ″ ″ 53 60 8 LSLRGLPV  976 A*0201 36 ″ 38 26 ″ ″ 53 60 8 LSLRGLPV ″ B*5201 33 ″ 35 26 ″ ″ 52 61 10 HLSLRGLPVC  977 A*3001 88 0,87 77 26 ″ ″ 53 61 9 LSLRGLPVC  978 B*5802 10 ″ 9 26 ″ ″ 53 63 11 LSLRGLPVCAF  979 B*1502 71 1,48 106 26 ″ ″ 53 63 11 LSLRGLPVCAF ″ B*1525 85 ″ 125 26 ″ ″ 53 63 11 LSLRGLPVCAF ″ B*4601 50 ″ 74 26 ″ ″ 53 63 11 LSLRGLPVCAF ″ B*5701 100 ″ 148 26 ″ ″ 53 63 11 LSLRGLPVCAF ″ B*5801 90 ″ 133 26 ″ ″ 53 63 11 LSLRGLPVCAF ″ B*5802 30 ″ 44 26 ″ ″ 54 63 10 SLRGIPVCAF  980 A*0301 100 ″ 148 26 ″ ″ 54 63 10 SLRGLPVCAF  981 B*1501 86 ″ 127 26 ″ ″ 54 63 10 SLRGLPVCAF ″ B*1502 86 ″ 127 26 ″ ″ 54 63 10 SLRGLPVCAF ″ B*1525 54 ″ 80 26 ″ ″ 54 63 10 SLRGLPVCAF ″ B*4601 36 ″ 53 26 ″ ″ 56 63 8 RGLPVCAF  982 A*2301 25 ″ 37 26 ″ ″ 56 63 8 RGLPVCAF ″ A*3201 20 ″ 30 26 ″ ″ 58 65 8 LPVCAFSS  983 B*5101 45 0,59 27 26 ″ ″ 58 65 8 LPVCAFSS ″ B*5501 13 ″ 7 26 ″ ″ 58 65 8 LPVCAFSS ″ B*5601 31 ″ 18 26 ″ ″ 56 66 11 RGLPVCAFSSA  984 A*3001 29 0,95 28 26 ″ ″ 57 66 10 GLPVCAFSSA  985 A*0201 20 ″ 19 26 ″ ″ 58 66 9 LPVCAFSSA  986 B*3503 83 ″ 79 26 ″ ″ 58 66 9 LPVCAFSSA ″ B*5101 91 ″ 86 26 ″ ″ 58 66 9 LPVCAFSSA ″ B*5501 100 ″ 95 26 ″ ″ 58 66 9 LPVCAFSSA ″ B*5601 100 ″ 95 26 ″ ″ 58 67 10 LPVCAFSSAG  987 B*3501 58 0,11 6 26 ″ ″ 58 67 10 LPVCAFSSAG ″ B*3503 8 ″ 1 26 ″ ″ 58 67 10 LPVCAFSSAG ″ B*5501 19 ″ 2 26 ″ ″ Cumulative Class I-BCI 5422 score^(E): 61 70 10 CAFSSAGPCA  988 A*3001 76 0,45 35 27  61  95 61 71 11 CAFSSAGPCAL  989 B*1402 57 1,74 99 27 ″ ″ 61 71 11 CAFSSAGPCAL ″ B*3901 64 ″ 111 27 ″ ″ 61 71 11 CAFSSAGPCAL ″ B*4801 57 ″ 99 27 ″ ″ 63 71 9 FSSAGPCAL  990 B*3901 100 ″ 174 27 ″ ″ 63 71 9 FSSAGPCAL ″ B*4601 71 ″ 124 27 ″ ″ 62 72 11 AFSSAGPCALR  991 A*3101 40 1,24 50 27 ″ ″ 63 72 10 FSSAGPCALR  992 A*3303 60 ″ 74 27 ″ ″ 63 72 10 FSSAGPCALR ″ A*6801 100 ″ 124 27 ″ ″ 64 72 9 SSAGPCALR  993 A*3303 87 ″ 107 27 ″ ″ 64 72 9 SSAGPCALR ″ A*6801 56 ″ 69 27 ″ ″ 63 73 11 FSSAGPCALRF  994 A*0101 38 1,58 59 27 ″ ″ 63 73 11 FSSAGPCALRF ″ B*1501 14 ″ 23 27 ″ ″ 63 73 11 FSSAGPCALRF ″ B*1502 43 ″ 68 27 ″ ″ 63 73 11 FSSAGPCALRF ″ B*1525 15 ″ 24 27 ″ ″ 63 73 11 FSSAGPCALRF ″ B*3501 50 ″ 79 27 ″ ″ 63 73 11 FSSAGPCALRF ″ B*4601 86 ″ 136 27 ″ ″ 63 73 11 FSSAGPCALRF ″ B*5301 86 ″ 136 27 ″ ″ 63 73 11 FSSAGPCALRF ″ B*5701 67 ″ 105 27 ″ ″ 63 73 11 FSSAGPCALRF ″ B*5801 100 ″ 158 27 ″ ″ 63 73 11 FSSAGPCALRF ″ B*5802 50 ″ 79 27 ″ ″ 64 73 10 SSAGPCALRF  995 B*5802 20 ″ 32 27 ″ ″ 65 73 9 SAGPCALRF  996 A*0101 25 ″ 40 27 ″ ″ 65 73 9 SAGPCALRF ″ B*5701 17 ″ 26 27 ″ ″ 69 77 9 CALRFTSAR  997 A*3101 30 1,06 32 27 ″ ″ 69 77 9 CALRFTSAR ″ A*3303 100 ″ 106 27 ″ ″ 69 77 9 CALRFTSAR ″ A*6801 11 ″ 12 27 ″ ″ 69 77 9 CALRFTSAR ″ A*7401 100 ″ 106 27 ″ ″ 70 77 8 ALRFTSAR  998 A*3001 18 ″ 19 27 ″ ″ 70 77 8 ALRFTSAR ″ A*3101 70 ″ 74 27 ″ ″ 70 77 8 ALRFTSAR ″ A*3303 53 ″ 56 27 ″ ″ 70 77 8 ALRFTSAR ″ A*7401 90 ″ 95 27 ″ ″ 70 77 8 ALRFTSAR ″ A*0301 81 ″ 86 27 ″ ″ 69 78 10 CALRFTSARR  999 A*3101 90 1,59 143 27 ″ ″ 69 78 10 CALRFTSARR ″ A*3303 93 ″ 148 27 ″ ″ 69 78 10 CALRFTSARR ″ A*7401 60 ″ 95 27 ″ ″ 70 78 9 ALRFTSARR 1000 A*3101 20 ″ 32 27 ″ ″ 70 78 9 ALRFTSARR ″ A*3303 7 ″ 11 27 ″ ″ 70 78 9 ALRFTSARR ″ A*7401 80 ″ 127 27 ″ ″ 70 78 9 ALRFTSARR ″ A*0301 50 ″ 80 27 ″ ″ 71 78 8 LRFTSARR 1001 B*2705 10 ″ 16 27 ″ ″ 70 79 10 ALRFTSARRM 1002 B*0701 50 1,80 90 27 ″ ″ 70 79 10 ALRFTSARRM ″ B*0801 67 ″ 120 27 ″ ″ 71 79 9 LRFTSARRM 1003 B*1402 7 ″ 13 27 ″ ″ 71 79 9 LRFTSARRM ″ B*2702 75 ″ 135 27 ″ ″ 71 79 9 LRFTSARRM ″ B*2705 60 ″ 108 27 ″ ″ 77 84 8 RRMETTVN 1004 B*2702 38 0,84 31 27 ″ ″ 75 85 11 SARRMETTVNA 1005 A*3001 6 1,44 8 27 ″ ″ 77 85 9 RRMETTVNA 1006 B*2702 50 ″ 72 27 ″ ″ 77 85 9 RRMETTVNA ″ B*2705 40 ″ 58 27 ″ ″ 77 86 10 RRMETTVNAH 1007 B*2702 63 0,74 46 27 ″ ″ 79 86 8 METTVNAH 1008 A*6802 60 ″ 44 27 ″ ″ 79 86 8 METTVNAH ″ B*1801 67 ″ 49 27 ″ ″ 79 86 8 METTVNAH ″ B*4403 33 ″ 25 27 ″ ″ 77 87 11 RRMETTVNAHQ 1009 B*2702 25 0,30 7 27 ″ ″ 79 87 9 METTVNAHQ 1010 B*4403 44 ″ 13 27 ″ ″ 78 88 11 RMETTVNAHQI 1011 A*3201 40 0,68 27 27 ″ ″ 79 88 10 METTVNAHQI 1012 B*1301 100 ″ 68 27 ″ ″ 79 88 10 METTVNAHQI ″ B*1302 67 ″ 45 27 ″ ″ 79 88 10 METTVNAHQI ″ B*1801 33 ″ 23 27 ″ ″ 79 88 10 METTVNAHQI ″ B*3701 100 ″ 68 27 ″ ″ 79 88 10 METTVNAHQI ″ B*3801 100 ″ 68 27 ″ ″ 79 88 10 METTVNAHQI ″ B*4901 100 ″ 68 27 ″ ″ 79 88 10 METTVNAHQI ″ B*5001 100 ″ 68 27 ″ ″ 79 88 10 METTVNAHQI ″ B*5201 100 ″ 68 27 ″ ″ 80 88 9 ETTVNAHQI 1013 A*6802 40 ″ 27 27 ″ ″ 79 89 11 METTVNAHQIL 1014 B*1301 75 0,67 50 27 ″ ″ 79 89 11 METTVNAHQIL ″ B*1801 100 ″ 67 27 ″ ″ 79 89 11 METTVNAHQIL ″ B*3701 92 ″ 61 27 ″ ″ 79 89 11 METTVNAHQIL ″ B*3801 80 ″ 53 27 ″ ″ 79 89 11 METTVNAHQIL ″ B*4001 90 ″ 60 27 ″ ″ 79 89 11 METTVNAHQIL ″ B*4002 43 ″ 29 27 ″ ″ 79 89 11 METTVNAHQIL ″ B*4402 40 ″ 27 27 ″ ″ 79 89 11 METTVNAHQIL ″ B*4403 67 ″ 45 27 ″ ″ 79 89 11 METTVNAHQIL ″ B*4801 43 ″ 29 27 ″ ″ 79 89 11 METTVNAHQIL ″ B*4901 78 ″ 52 27 ″ ″ 79 89 11 METTVNAHQIL ″ B*5001 20 ″ 13 27 ″ ″ 80 89 10 ETTVNAHQIL 1015 A*2501 40 ″ 27 27 ″ ″ 81 91 11 TTVNAHQILPK 1016 A*1101 67 0,39 26 27 ″ ″ 81 91 11 TTVNAHQILPK ″ A*6801 44 ″ 17 27 ″ ″ 81 91 11 TTVNAHQILPK ″ A*0301 6 ″ 2 27 ″ ″ 82 91 10 TVNAHQILPK 1017 A*1101 92 ″ 36 27 ″ ″ 82 91 10 TVNAHQILPK ″ A*0301 100 ″ 39 27 ″ ″ 82 92 11 TVNAHQILPKV 1018 A*0201 27 1,32 36 27 ″ ″ 84 93 10 NAHQILPKVL 1019 B*0701 25 1,59 40 27 ″ ″ 85 93 9 AHQILPKVL 1020 B*3801 60 ″ 95 27 ″ ″ 85 93 9 AHQILPKVL ″ B*3901 18 ″ 29 27 ″ ″ 86 93 8 HQILPKVL 1021 B*3901 91 ″ 144 27 ″ ″ 86 93 8 HQILPKVL ″ B*4801 100 ″ 159 27 ″ ″ 86 95 10 HQILPKVLHK 1022 A*1101 42 1,60 67 27 ″ ″ 86 95 10 HQILPKVLHK ″ A*0301 33 ″ 53 27 ″ ″ 87 95 9 QILPKVLHK 1023 A*1101 50 ″ 80 27 ″ ″ 87 95 9 QILPKVLHK ″ A*0101 75 ″ 120 27 ″ ″ 87 95 9 QILPKVLHK ″ A*0301 100 ″ 160 27 ″ ″ 88 95 8 ILPKVLHK 1024 A*0201 82 ″ 131 27 ″ ″ 88 95 8 ILPKVLHK ″ A*0301 63 ″ 100 27 ″ ″ Cumulative Class I-BCI 6468 score: 86 93 8 HQILPKVL 1021 B*3901 91 ″ 144 28  86 120 86 93 8 HQILPKVL ″ B*4801 100 ″ 159 28 ″ ″ 86 95 10 HQILPKVLHK 1022 A*1101 42 1,60 67 28 ″ ″ 86 95 10 HQILPKVLHK ″ A*0301 33 ″ 53 28 ″ ″ 87 95 9 QILPKVLHK 1023 A*1101 50 ″ 80 28 ″ ″ 87 95 9 QILPKVLHK ″ A*0101 75 ″ 120 28 ″ ″ 87 95 9 QILPKVLHK ″ A*0301 100 ″ 160 28 ″ ″ 88 95 8 ILPKVLHK 1024 A*0201 82 ″ 131 28 ″ ″ 88 95 8 ILPKVLHK ″ A*0301 63 ″ 100 28 ″ ″ 86 96 11 HQILPKVLHKR 1025 A*3101 50 1,87 94 28 ″ ″ 86 96 11 HQILPKVLHKR ″ A*3303 47 ″ 87 28 ″ ″ 87 96 10 QILPKVLHKR 1026 A*3101 60 ″ 112 28 ″ ″ 87 96 10 QILPKVLHKR ″ A*3303 67 ″ 125 28 ″ ″ 88 96 9 ILPKVLHKR 1027 A*3303 27 ″ 50 28 ″ ″ 88 96 9 ILPKVLHKR ″ A*0301 75 ″ 141 28 ″ ″ 89 96 8 LPKVLHKR 1028 B*0701 42 ″ 78 28 ″ ″ 88 97 10 ILPKVLHKRT 1029 A*0201 30 0,47 14 28 ″ ″ 89 98 10 LPKVLHKRTL 1030 B*5101 64 1,61 103 28 ″ ″ 89 98 10 LPKV1HKRIL ″ B*0701 88 ″ 141 28 ″ ″ 89 98 10 LPKV1HKRIL ″ B*0801 100 ″ 161 28 ″ ″ 91 98 8 KVLHKRTL 1031 B*0801 10 ″ 16 28 ″ ″ 91 100 10 KVLHKRTLGL 1032 A*0201 70 1,91 134 28 ″ ″ 91 100 10 KVLHKRTLGL ″ B*0701 38 ″ 72 28 ″ ″ 91 100 10 KVLHKRTLGL ″ B*0801 33 ″ 64 28 ″ ″ 92 100 9 VLHKRTLGL 1033 A*0201 90 ″ 172 28 ″ ″ 92 100 9 VLHKRTLGL ″ B*0801 100 ″ 191 28 ″ ″ 92 102 11 VLHKRTLGLSA 1034 B*0801 70 1,09 76 28 ″ ″ 95 102 8 KRTLGLSA 1035 B*2702 13 ″ 14 28 ″ ″ 93 103 11 LHKRTLGLSAM 1036 B*1402 86 1,72 148 28 ″ ″ 93 103 11 LHKRTLGLSAM ″ B*0801 20 ″ 34 28 ″ ″ 94 103 10 HKRTLGLSAM 1037 B*1402 50 ″ 86 28 ″ ″ 95 103 9 KRTLGLSAM 1038 B*2702 88 ″ 151 28 ″ ″ 96 103 8 RTLGLSAM 1039 A*2501 20 ″ 34 28 ″ ″ 96 103 8 RTLGLSAM ″ A*3201 100 ″ 172 28 ″ ″ 96 103 8 RTLGLSAM ″ B*1502 29 ″ 49 28 ″ ″ 96 103 8 RTLGLSAM ″ B*1525 23 ″ 40 28 ″ ″ 96 103 8 RTLGLSAM ″ B*4601 93 ″ 160 28 ″ ″ 96 103 8 RTLGLSAM ″ B*5701 33 ″ 57 28 ″ ″ 96 103 8 RTLGLSAM ″ B*5801 80 ″ 138 28 ″ ″ 97 104 8 TLGLSAMS 1040 A*0201 9 0,51 5 28 ″ ″ 97 105 9 TLGLSAMST 1041 A*0201 50 0,88 44 28 ″ ″ 97 106 10 TLGLSAMSTT 1042 A*0201 40 0,27 11 28 ″ ″ 99 108 10 GLSAMSTTDL 1043 A*0201 50 1,60 80 28 ″ ″ 100 110 11 LSAMSTTDLEA 1044 A*0206 100 1,07 107 28 ″ ″ 101 111 11 SAMSTTDLEAY 1045 A*2902 75 0,70 53 28 ″ ″ 101 111 11 SAMSTTDLEAY ″ A*3002 100 ″ 70 28 ″ ″ 101 111 11 SAMSTTDLEAY ″ B*1501 100 ″ 70 28 ″ ″ 101 111 11 SAMSTTDLEAY ″ B*1502 100 ″ 70 28 ″ ″ 101 111 11 SAMSTTDLEAY ″ B*1525 100 ″ 70 28 ″ ″ 101 111 11 SAMSTTDLEAY ″ B*4601 100 ″ 70 28 ″ ″ 101 111 11 SAMSTTDLEAY ″ B*5301 57 ″ 40 28 ″ ″ 101 111 11 SAMSTTDLEAY ″ B*5801 60 ″ 42 28 ″ ″ 102 111 10 AMSTTDLEAY 1046 A*0301 50 ″ 35 28 ″ ″ 103 111 9 MSTTDLEAY 1047 A*2601 25 ″ 18 28 ″ ″ 103 111 9 MSTTDLEAY ″ A*0101 88 ″ 62 28 ″ ″ 103 111 9 MSTTDLEAY ″ B*3501 83 ″ 59 28 ″ ″ 104 111 8 STTDLEAY 1048 A*2501 100 ″ 70 28 ″ ″ 102 112 11 AMSTTDLEAYF 1049 A*3002 20 1,45 29 28 ″ ″ 102 112 11 AMSTTDLEAYF ″ B*1501 71 ″ 104 28 ″ ″ 102 112 11 AMSTTDLEAYF ″ B*1502 14 ″ 21 28 ″ ″ 102 112 11 AMSTTDLEAYF ″ B*1525 62 ″ 89 28 ″ ″ 102 112 11 AMSTTDLEAYF ″ B*4601 7 ″ 10 28 ″ ″ 103 112 10 MSTTDLEAYF 1050 A*0101 13 ″ 18 28 ″ ″ 103 112 10 MSTTDLEAYF ″ B*3501 42 ″ 61 28 ″ ″ 103 112 10 MSTTDLEAYF ″ B*4601 43 ″ 62 28 ″ ″ 103 112 10 MSTTDLEAYF ″ B*5301 14 ″ 21 28 ″ ″ 103 112 10 MSTTDLEAYF ″ B*5802 40 ″ 58 28 ″ ″ 104 112 9 STTDLEAYF 1051 A*2501 60 ″ 87 28 ″ ″ 104 112 9 STTDLEAYF ″ A*2601 50 ″ 73 28 ″ ″ 105 112 8 TTDLEAYF 1052 A*0101 75 ″ 109 28 ″ ″ 103 113 11 MSTTDLEAYFK 1053 A*1101 75 0,43 32 28 ″ ″ 103 113 11 MSTTDLEAYFK ″ A*6801 67 ″ 29 28 ″ ″ 104 113 10 STTDLEAYFK 1054 A*1101 100 ″ 43 28 ″ ″ 104 113 10 STTDLEAYFK ″ A*6801 89 ″ 38 28 ″ ″ 104 113 10 STTDLEAYFK ″ A*0301 19 ″ 8 28 ″ ″ 105 113 9 TTDLEAYFK 1055 A*1101 83 ″ 36 28 ″ ″ 105 113 9 TTDLEAYFK ″ A*6801 22 ″ 10 28 ″ ″ 105 113 9 TTDLEAYFK ″ A*0101 100 ″ 43 28 ″ ″ 105 113 9 TTDLEAYFK ″ A*0301 25 ″ 11 28 ″ ″ 106 116 11 TDLEAYFKDCV 1056 A*0201 64 0,18 12 28 ″ ″ 106 116 11 TDLEAYFKDCV ″ B*3701 33 ″ 6 28 ″ ″ 108 116 9 LEAYFKDCV 1057 A*0201 10 ″ 2 28 ″ ″ 108 116 9 LEAYFKDCV ″ B*1301 25 ″ 5 28 ″ ″ 108 116 9 LEAYFKDCV ″ B*3701 75 ″ 14 28 ″ ″ 108 116 9 LEAYFKDCV ″ B*4001 40 ″ 7 28 ″ ″ 108 116 9 LEAYFKDCV ″ B*4901 89 ″ 16 28 ″ ″ 108 116 9 LEAYFKDCV ″ B*5001 80 ″ 15 28 ″ ″ 109 116 8 EAYFKDCV 1058 B*0801 40 ″ 7 28 ″ ″ 108 117 10 LEAYFKDCVF 1059 B*1301 63 1,37 85 28 ″ ″ 108 117 10 LEAYFKDCVF ″ B*3701 42 ″ 57 28 ″ ″ 108 117 10 LEAYFKDCVF ″ B*4001 20 ″ 27 28 ″ ″ 108 117 10 LEAYFKDCVF ″ B*4402 80 ″ 109 28 ″ ″ 108 117 10 LEAYFKDCVF ″ B*4403 89 ″ 121 28 ″ ″ 108 117 10 LEAYFKDCVF ″ B*4901 67 ″ 91 28 ″ ″ 108 117 10 LEAYFKDCVF ″ B*5001 60 ″ 82 28 ″ ″ 110 117 8 AYFKDCVF 1060 A*2301 100 ″ 137 28 ″ ″ 110 117 8 AYFKDCVF ″ A*2402 100 ″ 137 28 ″ ″ 109 118 10 EAYFKDCVFK 1061 A*1101 25 1,38 34 28 ″ ″ 109 118 10 EAYFKDCVFK ″ A*6801 78 ″ 107 28 ″ ″ 110 118 9 AYFKDCVFK 1062 A*1101 8 ″ 11 28 ″ ″ 111 118 8 YFKDCVFK 1063 A*3101 10 ″ 14 28 ″ ″ 111 118 8 YFKDCVFK ″ A*3303 80 ″ 110 28 ″ ″ 110 120 11 AYFKDCVFKDW 1064 A*2301 75 1,74 131 28 ″ ″ 110 120 11 AYFKDCVFKDW ″ A*2402 67 ″ 116 28 ″ ″ Cumulative Class I-BCI 7354 score: 108 117 10 LEAYFKDCVF 1059 B*1301 63 1,37 85 29 108 141 108 117 10 LEAYFKDCVF ″ B*3701 42 ″ 57 29 ″ ″ 108 117 10 LEAYFKDCVF ″ B*4001 20 ″ 27 29 ″ ″ 108 117 10 LEAYFKDCVF ″ B*4402 80 ″ 109 29 ″ ″ 108 117 10 LEAYFKDCVF ″ B*4403 89 ″ 121 29 ″ ″ 108 117 10 LEAYFKDCVF ″ B*4901 67 ″ 91 29 ″ ″ 108 117 10 LEAYFKDCVF ″ B*5001 60 ″ 82 29 ″ ″ 110 117 8 AYFKDCVF 1060 A*2301 100 ″ 137 29 ″ ″ 110 117 8 AYFKDCVF ″ A*2402 100 ″ 137 29 ″ ″ 109 118 10 EAYFKDCVFK 1061 A*1101 25 1,38 34 29 ″ ″ 109 118 10 EAYFKDCVFK ″ A*6801 78 ″ 107 29 ″ ″ 110 118 9 AYFKDCVFK 1062 A*1101 8 ″ 11 29 ″ ″ 111 118 8 YFKDCVFK 1063 A*3101 10 ″ 14 29 ″ ″ 111 118 8 YFKDCVFK ″ A*3303 80 ″ 110 29 ″ ″ 110 120 11 AYFKDCVFKDW 1064 A*2301 75 1,74 131 29 ″ ″ 110 120 11 AYFKDCVFKDW ″ A*2402 67 ″ 116 29 ″ ″ 114 123 10 DCVFKDWEEL 1065 A*3201 60 1,30 78 29 ″ ″ 115 123 9 CVFKDWEEL 1066 A*0201 40 ″ 52 29 ″ ″ 115 123 9 CVFKDWEEL ″ B*0701 50 ″ 65 29 ″ ″ 118 127 10 KDWEELGEEI 1067 B*1301 88 0,73 63 29 ″ ″ 118 127 10 KDWEELGEEI ″ B*1302 100 ″ 73 29 ″ ″ 118 127 10 KDWEELGEEI ″ B*5201 67 ″ 48 29 ″ ″ 120 127 8 WEELGEEI 1068 B*1301 50 ″ 36 29 ″ ″ 120 127 8 WEELGEEI ″ B*4001 70 ″ 51 29 ″ ″ 120 127 8 WEELGEEI ″ B*4901 56 ″ 40 29 ″ ″ 119 129 11 DWEELGEEIRL 1069 A*0201 55 1,70 93 29 ″ ″ 120 129 10 WEELGEEIRL 1070 B*3801 20 ″ 34 29 ″ ″ 120 129 10 WEELGEEIRL ″ B*4001 10 ″ 17 29 ″ ″ 121 129 9 EELGEEIRL 1071 B*4001 60 ″ 102 29 ″ ″ 121 129 9 EELGEEIRL ″ B*4403 22 ″ 38 29 ″ ″ 121 131 11 EELGEEIRLKV 1072 B*1801 17 1,00 17 29 ″ ″ 121 131 11 EELGEEIRLKV ″ B*3701 50 ″ 50 29 ″ ″ 122 131 10 ELGEEIRLKV 1073 A*0201 60 ″ 60 29 ″ ″ 124 131 8 GEEIRLKV 1074 B*4901 11 ″ 11 29 ″ ″ 123 132 10 LGEEIRLKVF 1075 A*0101 50 1,36 68 29 ″ ″ 124 132 9 GEEIRLKVF 1076 B*4402 60 ″ 82 29 ″ ″ 124 132 9 GEEIRLKVF ″ B*4403 11 ″ 15 29 ″ ″ 125 132 8 EEIRLKVF 1077 B*1801 83 ″ 113 29 ″ ″ 125 132 8 EEIRLKVF ″ B*4402 20 ″ 27 29 ″ ″ 125 132 8 EEIRLKVF ″ B*4403 56 ″ 75 29 ″ ″ 123 133 11 LGEEIRLKVFV 1078 A*0206 50 1,07 54 29 ″ ″ 123 133 11 LGEEIRLKVFV ″ A*0201 91 ″ 98 29 ″ ″ 125 133 9 EEIRLKVFV 1079 B*3701 58 ″ 63 29 ″ ″ 125 133 9 EEIRLKVFV ″ B*4001 30 ″ 32 29 ″ ″ 125 133 9 EEIRLKVFV ″ B*4403 78 ″ 84 29 ″ ″ 126 133 8 EIRLKVFV 1080 B*0801 100 ″ 107 29 ″ ″ 125 134 10 EEIRLKVFVL 1081 B*1801 50 1,85 93 29 ″ ″ 125 134 10 EEIRLKVFVL ″ B*3701 83 ″ 154 29 ″ ″ 125 134 10 EEIRLKVFVL ″ B*3801 40 ″ 74 29 ″ ″ 125 134 10 EEIRLKVFVL ″ B*4001 100 ″ 185 29 ″ ″ 125 134 10 EEIRLKVFVL ″ B*4002 71 ″ 132 29 ″ ″ 125 134 10 EEIRLKVFVL ″ B*4402 100 ″ 185 29 ″ ″ 125 134 10 EEIRLKVFVL ″ B*4403 100 ″ 185 29 ″ ″ 126 134 9 EIRLKVFVL 1082 B*0701 63 ″ 116 29 ″ ″ 126 134 9 EIRLKVFVL ″ B*0801 100 ″ 185 29 ″ ″ 127 134 8 IRLKVFVL 1083 A*0206 25 ″ 46 29 ″ ″ 127 134 8 IRLKVFVL ″ B*1402 64 ″ 119 29 ″ ″ 127 134 8 IRLKVFVL ″ B*2702 100 ″ 185 29 ″ ″ 127 134 8 IRLKVFVL ″ B*3901 82 ″ 151 29 ″ ″ 129 136 8 LKVFVLGG 1084 A*0206 75 0,47 35 29 ″ ″ 128 138 11 RLKVFVLGGCR 1085 A*3101 80 0,64 51 29 ″ ″ 128 138 11 RLKVFVLGGCR ″ A*7401 30 ″ 19 29 ″ ″ 128 138 11 RLKVFVLGGCR ″ A*0301 13 ″ 8 29 ″ ″ 130 138 9 KVFVLGGCR 1086 A*3101 100 ″ 64 29 ″ ″ 130 138 9 KVFVLGGCR ″ A*7401 50 ″ 32 29 ″ ″ 130 140 11 KVFVLGGCRHK 1087 A*1101 58 1,05 61 29 ″ ″ 130 140 11 KVFVLGGCRHK ″ A*3001 94 ″ 99 29 ″ ″ 130 140 11 KVFVLGGCRHK ″ A*0301 94 ″ 98 29 ″ ″ 133 140 8 VLGGCRHK 1088 A*0201 18 ″ 19 29 ″ ″ 133 140 8 VLGGCRHK ″ A*0301 44 ″ 46 29 ″ ″ 132 141 10 FVLGGCRHKL 1089 A*0201 80 1,66 133 29 ″ ″ 132 141 10 FVLGGCRHKL ″ B*0701 63 ″ 104 29 ″ ″ 133 141 9 VLGGCRHKL 1090 A*0201 100 ″ 166 29 ″ ″ Cumulative Class I-BCI 5862 score: ″Start″ and ″End″ are relative to the amino acid sequence of HBV X protein, consensus sequence, as depicted in SEQ ID NO: 45 ^(A)Peptide amino acid sequence. Each HLA class I binding peptide of HBV X protein is listed separately for each HLA class I molecule to which it is predicted to bind, and can be listed multiple times for that reason. ^(B)Class I-B score. See Material and Methods (Examples section). ^(C)C-score. See Material and Methods (Examples section). ^(D)Class I-BCI score. See Material and Methods (Examples section). ^(E)Cumulative Class I-BCI score. See Material and Methods (Examples section).

TABLE 6b Predicted HLA class II-restricted CD4⁺ T cell epitopes contained in SLP sequences from HBV X protein (consensus sequence). HLA class II binding peptides in SLP derived from HBV X protein (consens. seq) Peptide of invention HLA- Class (SLP) SEQ ID DRB1 II-B SLP SLP Start End Sequence^(A) NO: molecule score^(B) SLP # Start End 46 60 PADHGAHLSLRGLPV 1091 *0701 8 26 36 68 47 61 ADHGAHLSLRGLPVC 1092 *0101 13 26 ″ ″ 47 61 ADHGAHLSLRGLPVC ″ *0102 20 26 ″ ″ 47 61 ADHGAHLSLRGLPVC ″ *0105 13 26 ″ ″ 47 61 ADHGAHLSLRGLPVC ″ *0107 13 26 ″ ″ 48 62 DHGAHLSLRGLPVCA 1093 *0101 87 26 ″ ″ 48 62 DHGAHLSLRGLPVCA ″ *0102 67 26 ″ ″ 48 62 DHGAHLSLRGLPVCA ″ *0104 43 26 ″ ″ 48 62 DHGAHLSLRGLPVCA ″ *0105 87 26 ″ ″ 48 62 DHGAHLSLRGLPVCA ″ *0106 53 26 ″ ″ 48 62 DHGAHLSLRGLPVCA ″ *0107 87 26 ″ ″ 49 63 HGAHLSLRGLPVCAF 1094 *0101 100 26 ″ ″ 49 63 HGAHLSLRGLPVCAF ″ *0102 93 26 ″ ″ 49 63 HGAHLSLRGLPVCAF ″ *0103 40 26 ″ ″ 49 63 HGAHLSLRGLPVCAF ″ *0104 90 26 ″ ″ 49 63 HGAHLSLRGLPVCAF ″ *0105 90 26 ″ ″ 49 63 HGAHLSLRGLPVCAF ″ *0106 90 26 ″ ″ 49 63 HGAHLSLRGLPVCAF ″ *0107 90 26 ″ ″ 49 63 HGAHLSLRGLPVCAF ″ *1101 85 26 ″ ″ 49 63 HGAHLSLRGLPVCAF ″ *1301 100 26 ″ ″ 49 63 HGAHLSLRGLPVCAF ″ *1501 46 26 ″ ″ 50 64 GAHLSLRGLPVCAFS 1095 *0101 77 26 ″ ″ 50 64 GAHLSLRGLPVCAFS ″ *0102 97 26 ″ ″ 50 64 GAHLSLRGLPVCAFS ″ *0103 70 26 ″ ″ 50 64 GAHLSLRGLPVCAFS ″ *0104 93 26 ″ ″ 50 64 GAHLSLRGLPVCAFS ″ *0105 93 26 ″ ″ 50 64 GAHLSLRGLPVCAFS ″ *0106 97 26 ″ ″ 50 64 GAHLSLRGLPVCAFS ″ *0107 93 26 ″ ″ 50 64 GAHLSLRGLPVCAFS ″ *1101 77 26 ″ ″ 50 64 GAHLSLRGLPVCAFS ″ *1301 92 26 ″ ″ 50 64 GAHLSLRGLPVCAFS ″ *1501 54 26 ″ ″ 51 65 AHLSLRGLPVCAFSS 1096 *0101 100 26 ″ ″ 51 65 AHLSLRGLPVCAFSS ″ *0102 100 26 ″ ″ 51 65 AHLSLRGLPVCAFSS ″ *0103 100 26 ″ ″ 51 65 AHLSLRGLPVCAFSS ″ *0104 100 26 ″ ″ 51 65 AHLSLRGLPVCAFSS ″ *0105 100 26 ″ ″ 51 65 AHLSLRGLPVCAFSS ″ *0106 100 26 ″ ″ 51 65 AHLSLRGLPVCAFSS ″ *0107 100 26 ″ ″ 51 65 AHLSLRGLPVCAFSS ″ *1301 85 26 ″ ″ 52 66 HLSLRGLPVCAFSSA 1097 *0101 97 26 ″ ″ 52 66 HLSLRGLPVCAFSSA ″ *0102 90 26 ″ ″ 52 66 HLSLRGLPVCAFSSA ″ *0103 90 26 ″ ″ 52 66 HLSLRGLPVCAFSSA ″ *0104 97 26 ″ ″ 52 66 HLSLRGLPVCAFSSA ″ *0105 97 26 ″ ″ 52 66 HLSLRGLPVCAFSSA ″ *0106 93 26 ″ ″ 52 66 HLSLRGLPVCAFSSA ″ *0107 97 26 ″ ″ 52 66 HLSLRGLPVCAFSSA ″ *1301 77 26 ″ ″ 53 67 LSLRGLPVCAFSSAG 1098 *0101 83 26 ″ ″ 53 67 LSLRGLPVCAFSSAG ″ *0102 50 26 ″ ″ 53 67 LSLRGLPVCAFSSAG ″ *0104 77 26 ″ ″ 53 67 LSLRGLPVCAFSSAG ″ *0105 83 26 ″ ″ 53 67 LSLRGLPVCAFSSAG ″ *0106 73 26 ″ ″ 53 67 LSLRGLPVCAFSSAG ″ *0107 83 26 ″ ″ 53 67 LSLRGLPVCAFSSAG ″ *1301 69 26 ″ ″ 54 68 SLRGLPVCAFSSAGP 1099 *0101 37 26 ″ ″ 54 68 SLRGLPVCAFSSAGP ″ *0102 7 26 ″ ″ 54 68 SLRGLPVCAFSSAGP ″ *0104 30 26 ″ ″ 54 68 SLRGLPVCAFSSAGP ″ *0105 37 26 ″ ″ 54 68 SLRGLPVCAFSSAGP ″ *0106 7 26 ″ ″ 54 68 SLRGLPVCAFSSAGP ″ *0107 37 26 ″ ″ 54 68 SLRGLPVCAFSSAGP ″ *1301 62 26 ″ ″ Cumulative Class II-B score^(C): 4414 61 75 CAFSSAGPCALRFTS 1100 *0101 20 27 61 95 61 75 CAFSSAGPCALRFTS ″ *0105 20 27 ″ ″ 61 75 CAFSSAGPCALRFTS ″ *0107 20 27 ″ ″ 61 75 CAFSSAGPCALRFTS ″ *0701 15 27 ″ ″ 64 78 SSAGPCALRFTSARR 1101 *1501 69 27 ″ ″ 65 79 SAGPCALRFTSARRM 1102 *0101 23 27 ″ ″ 65 79 SAGPCALRFTSARRM ″ *0102 23 27 ″ ″ 65 79 SAGPCALRFTSARRM ″ *0104 27 27 ″ ″ 65 79 SAGPCALRFTSARRM ″ *0106 23 27 ″ ″ 65 79 SAGPCALRFTSARRM ″ *0401 31 27 ″ ″ 65 79 SAGPCALRFTSARRM ″ *0701 85 27 ″ ″ 65 79 SAGPCALRFTSARRM ″ *1301 46 27 ″ ″ 65 79 SAGPCALRFTSARRM ″ *1501 92 27 ″ ″ 66 80 AGPCALRFTSARRME 1103 *0101 69 27 ″ ″ 66 80 AGPCALRFTSARRME ″ *0102 37 27 ″ ″ 66 80 AGPCALRFTSARRME ″ *0104 40 27 ″ ″ 66 80 AGPCALRFTSARRME ″ *0105 3 27 ″ ″ 66 80 AGPCALRFTSARRME ″ *0106 37 27 ″ ″ 66 80 AGPCALRFTSARRME ″ *0107 3 27 ″ ″ 66 80 AGPCALRFTSARRME ″ *0401 46 27 ″ ″ 66 80 AGPCALRFTSARRME ″ *0701 69 27 ″ ″ 66 80 AGPCALRFTSARRME ″ *1301 38 27 ″ ″ 66 80 AGPCALRFTSARRME ″ *1501 85 27 ″ ″ 67 81 GPCALRFTSARRMET 1104 *0101 62 27 ″ ″ 67 81 GPCALRFTSARRMET ″ *0102 57 27 ″ ″ 67 81 GPCALRFTSARRMET ″ *0104 70 27 ″ ″ 67 81 GPCALRFTSARRMET ″ *0105 43 27 ″ ″ 67 81 GPCALRFTSARRMET ″ *0106 80 27 ″ ″ 67 81 GPCALRFTSARRMET ″ *0107 43 27 ″ ″ 67 81 GPCALRFTSARRMET ″ *0301 46 27 ″ ″ 67 81 GPCALRFTSARRMET ″ *0401 92 27 ″ ″ 67 81 GPCALRFTSARRMET ″ *0701 77 27 ″ ″ 67 81 GPCALRFTSARRMET ″ *1101 8 27 ″ ″ 67 81 GPCALRFTSARRMET ″ *1301 31 27 ″ ″ 67 81 GPCALRFTSARRMET ″ *1501 100 27 ″ ″ 68 82 PCALRFTSARRMETT 1105 *0101 54 27 ″ ″ 68 82 PCALRFTSARRMETT ″ *0102 60 27 ″ ″ 68 82 PCALRFTSARRMETT ″ *0104 83 27 ″ ″ 68 82 PCALRFTSARRMETT ″ *0105 57 27 ″ ″ 68 82 PCALRFTSARRMETT ″ *0106 83 27 ″ ″ 68 82 PCALRFTSARRMETT ″ *0107 57 27 ″ ″ 68 82 PCALRFTSARRMETT ″ *0301 38 27 ″ ″ 68 82 PCALRFTSARRMETT ″ *0401 69 27 ″ ″ 68 82 PCALRFTSARRMETT ″ *0701 100 27 ″ ″ 68 82 PCALRFTSARRMETT ″ *1101 31 27 ″ ″ 68 82 PCALRFTSARRMETT ″ *1301 23 27 ″ ″ 68 82 PCALRFTSARRMETT ″ *1501 77 27 ″ ″ 69 83 CALRFTSARRMETTV 1106 *0101 46 27 ″ ″ 69 83 CALRFTSARRMETTV ″ *0102 43 27 ″ ″ 69 83 CALRFTSARRMETTV ″ *0104 67 27 ″ ″ 69 83 CALRFTSARRMETTV ″ *0105 47 27 ″ ″ 69 83 CALRFTSARRMETTV ″ *0106 57 27 ″ ″ 69 83 CALRFTSARRMETTV ″ *0107 47 27 ″ ″ 69 83 CALRFTSARRMETTV ″ *0301 31 27 ″ ″ 69 83 CALRFTSARRMETTV ″ *0401 23 27 ″ ″ 69 83 CALRFTSARRMETTV ″ *0701 92 27 ″ ″ 69 83 CALRFTSARRMETTV ″ *1101 38 27 ″ ″ 69 83 CALRFTSARRMETTV ″ *1301 15 27 ″ ″ 69 83 CALRFTSARRMETTV ″ *1501 62 27 ″ ″ 70 84 ALRFTSARRMETTVN 1107 *0101 38 27 ″ ″ 70 84 ALRFTSARRMETTVN ″ *0102 17 27 ″ ″ 70 84 ALRFTSARRMETTVN ″ *0104 37 27 ″ ″ 70 84 ALRFTSARRMETTVN ″ *0106 3 27 ″ ″ 70 84 ALRFTSARRMETTVN ″ *0301 62 27 ″ ″ 70 84 ALRFTSARRMETTVN ″ *0401 8 27 ″ ″ 70 84 ALRFTSARRMETTVN ″ *0701 62 27 ″ ″ 70 84 ALRFTSARRMETTVN ″ *1101 46 27 ″ ″ 70 84 ALRFTSARRMETTVN ″ *1301 8 27 ″ ″ 70 84 ALRFTSARRMETTVN ″ *1501 23 27 ″ ″ 71 85 LRFTSARRMETTVNA 1108 *0301 23 27 ″ ″ 71 85 LRFTSARRMETTVNA ″ *0401 15 27 ″ ″ 71 85 LRFTSARRMETTVNA ″ *0701 54 27 ″ ″ 71 85 LRFTSARRMETTVNA ″ *1101 23 27 ″ ″ 73 87 FTSARRMETTVNAHQ 1109 *0401 85 27 ″ ″ 74 88 TSARRMETTVNAHQI 1110 *0401 100 27 ″ ″ 75 89 SARRMETTVNAHQIL 1111 *0401 38 27 ″ ″ 75 89 SARRMETTVNAHQIL ″ *1301 40 27 ″ ″ 76 90 ARRMETTVNAHQILP 1112 *0401 80 27 ″ ″ 76 90 ARRMETTVNAHQILP ″ *1301 10 27 ″ ″ 77 91 RRMETTVNAHQILPK 1113 *1301 50 27 ″ ″ 78 92 RMETTVNAHQILPKV 1114 *1301 20 27 ″ ″ 81 95 TTVNAHQILPKVLHK 1115 *1101 15 27 ″ ″ Cumulative Class II-B score: 3788 86 100 HQILPKVLHKRTLGL 1116 *1101 54 28 86 120 87 101 QILPKVLHKRTLGLS 1117 *0102 10 28 ″ ″ 87 101 QILPKVLHKRTLGLS ″ *1101 22 28 ″ ″ 87 101 QILPKVLHKRTLGLS ″ *1301 70 28 ″ ″ 88 102 ILPKVLHKRTLGLSA 1118 *0102 53 28 ″ ″ 88 102 ILPKVLHKRTLGLSA ″ *0104 17 28 ″ ″ 88 102 ILPKVLHKRTLGLSA ″ *0106 33 28 ″ ″ 88 102 ILPKVLHKRTLGLSA ″ *1101 44 28 ″ ″ 88 102 ILPKVLHKRTLGLSA ″ *1301 80 28 ″ ″ 89 103 LPKVLHKRTLGLSAM 1119 *0101 10 28 ″ ″ 89 103 LPKVLHKRTLGLSAM ″ *0102 77 28 ″ ″ 89 103 LPKVLHKRTLGLSAM ″ *0104 60 28 ″ ″ 89 103 LPKVLHKRTLGLSAM ″ *0105 10 28 ″ ″ 89 103 LPKVLHKRTLGLSAM ″ *0106 77 28 ″ ″ 89 103 LPKVLHKRTLGLSAM ″ *0107 10 28 ″ ″ 89 103 LPKVLHKRTLGLSAM ″ *0701 10 28 ″ ″ 89 103 LPKVLHKRTLGLSAM ″ *1101 78 28 ″ ″ 89 103 LPKVLHKRTLGLSAM ″ *1301 100 28 ″ ″ 89 103 LPKVLHKRTLGLSAM ″ *1501 40 28 ″ ″ 90 104 PKVLHKRTLGLSAMS 1120 *0101 33 28 ″ ″ 90 104 PKVLHKRTLGLSAMS ″ *0102 73 28 ″ ″ 90 104 PKVLHKRTLGLSAMS ″ *0104 63 28 ″ ″ 90 104 PKVLHKRTLGLSAMS ″ *0105 33 28 ″ ″ 90 104 PKVLHKRTLGLSAMS ″ *0106 67 28 ″ ″ 90 104 PKVLHKRTLGLSAMS ″ *0107 33 28 ″ ″ 90 104 PKVLHKRTLGLSAMS ″ *1101 72 28 ″ ″ 90 104 PKVLHKRTLGLSAMS ″ *1301 90 28 ″ ″ 91 105 KVLHKRTLGLSAMST 1121 *0101 63 28 ″ ″ 91 105 KVLHKRTLGLSAMST ″ *0102 70 28 ″ ″ 91 105 KVLHKRTLGLSAMST ″ *0104 50 28 ″ ″ 91 105 KVLHKRTLGLSAMST ″ *0105 63 28 ″ ″ 91 105 KVLHKRTLGLSAMST ″ *0106 60 28 ″ ″ 91 105 KVLHKRTLGLSAMST ″ *0107 63 28 ″ ″ 91 105 KVLHKRTLGLSAMST ″ *1101 11 28 ″ ″ 91 105 KVLHKRTLGLSAMST ″ *1301 60 28 ″ ″ 92 106 VLHKRTLGLSAMSTT 1122 *0101 15 28 ″ ″ 92 106 VLHKRTLGLSAMSTT ″ *0102 47 28 ″ ″ 92 106 VLHKRTLGLSAMSTT ″ *0104 23 28 ″ ″ 92 106 VLHKRTLGLSAMSTT ″ *0105 73 28 ″ ″ 92 106 VLHKRTLGLSAMSTT ″ *0106 43 28 ″ ″ 92 106 VLHKRTLGLSAMSTT ″ *0107 73 28 ″ ″ 93 107 LHKRTLGLSAMSTTD 1123 *0101 60 28 ″ ″ 93 107 LHKRTLGLSAMSTTD ″ *0102 27 28 ″ ″ 93 107 LHKRTLGLSAMSTTD ″ *0105 60 28 ″ ″ 93 107 LHKRTLGLSAMSTTD ″ *0107 60 28 ″ ″ 94 108 HKRTLGLSAMSTTDL 1124 *0101 92 28 ″ ″ 94 108 HKRTLGLSAMSTTDL ″ *0102 33 28 ″ ″ 94 108 HKRTLGLSAMSTTDL ″ *0104 3 28 ″ ″ 94 108 HKRTLGLSAMSTTDL ″ *0105 67 28 ″ ″ 94 108 HKRTLGLSAMSTTDL ″ *0106 40 28 ″ ″ 94 108 HKRTLGLSAMSTTDL ″ *0107 67 28 ″ ″ 94 108 HKRTLGLSAMSTTDL ″ *0401 77 28 ″ ″ 95 109 KRTLGLSAMSTTDLE 1125 *0101 31 28 ″ ″ 95 109 KRTLGLSAMSTTDLE ″ *0105 23 28 ″ ″ 95 109 KRTLGLSAMSTTDLE ″ *0106 17 28 ″ ″ 95 109 KRTLGLSAMSTTDLE ″ *0107 23 28 ″ ″ 95 109 KRTLGLSAMSTTDLE ″ *0401 54 28 ″ ″ 96 110 RTLGLSAMSTTDLEA 1126 *0101 8 28 ″ ″ 96 110 RTLGLSAMSTTDLEA ″ *0105 30 28 ″ ″ 96 110 RTLGLSAMSTTDLEA ″ *0106 27 28 ″ ″ 96 110 RTLGLSAMSTTDLEA ″ *0107 30 28 ″ ″ 96 110 RTLGLSAMSTTDLEA ″ *0401 62 28 ″ ″ 97 111 TLGLSAMSTTDLEAY 1127 *0101 17 28 ″ ″ 97 111 TLGLSAMSTTDLEAY ″ *0105 17 28 ″ ″ 97 111 TLGLSAMSTTDLEAY ″ *0106 20 28 ″ ″ 97 111 TLGLSAMSTTDLEAY ″ *0107 17 28 ″ ″ 97 111 TLGLSAMSTTDLEAY ″ *0401 50 28 ″ ″ 105 119 TTDLEAYFKDCVFKD 1128 *0301 69 28 ″ ″ 106 120 TDLEAYFKDCVFKDW 1129 *0301 54 28 ″ ″ Cumulative Class II-B score: 3170 108 122 LEAYFKDCVFKDWEE 1130 *0301 15 29 108 141 110 124 AYFKDCVFKDWEELG 1131 *0301 100 29 ″ ″ 111 125 YFKDCVFKDWEELGE 1132 *0301 92 29 ″ ″ 119 133 DWEELGEEIRLKVFV 1133 *0301 77 29 ″ ″ 120 134 WEELGEEIRLKVFVL 1134 *0301 85 29 ″ ″ 120 134 WEELGEEIRLKVFVL ″ *1501 8 29 ″ ″ 121 135 EELGEEIRLKVFVLG 1135 *1501 31 29 ″ ″ 123 137 LGEEIRLKVFVLGGC 1136 *1501 15 29 ″ ″ 124 138 GEEIRLKVFVLGGCR 1137 *1501 38 29 ″ ″ 125 139 EEIRLKVFVLGGCRH 1138 *0102 3 29 ″ ″ 126 140 EIRLKVFVLGGCRHK 1139 *0102 40 29 ″ ″ 126 140 EIRLKVFVLGGCRHK ″ *0104 20 29 ″ ″ 126 140 EIRLKVFVLGGCRHK ″ *1501 10 29 ″ ″ 127 141 IRLKVFVLGGCRHKL 1140 *0101 40 29 ″ ″ 127 141 IRLKVFVLGGCRHKL ″ *0102 80 29 ″ ″ 127 141 IRLKVFVLGGCRHKL ″ *0104 73 29 ″ ″ 127 141 IRLKVFVLGGCRHKL ″ *0105 40 29 ″ ″ 127 141 IRLKVFVLGGCRHKL ″ *0106 70 29 ″ ″ 127 141 IRLKVFVLGGCRHKL ″ *0107 40 29 ″ ″ 127 141 IRLKVFVLGGCRHKL ″ *1101 56 29 ″ ″ 127 141 IRLKVFVLGGCRHKL ″ *1501 90 29 ″ ″ Cumulative Class II-B score: 1024 ″Start″ and ″End″ are relative to the amino acid sequence of human HBV X protein as depicted in SEQ ID NO: 45 ^(A)Peptide amino acid sequence. Each HLA-DRB1 binding peptide of HBV X protein is listed separately for each HLA class II molecule to which it is predicted to bind, and each peptide can be listed multiple times for that reason. ^(B)Class II-B score. See Material and Methods (Examples section). CCumulative Class II-B score. See Material and Methods (Examples section).

TABLE 7a Predidcted HLA class I-restricted CD8⁺ cytotoxic T cell epitopes contained in SLP sequences  from HBV large surgace protein. HLA class I binding peptides contained in SLP sequences derived from HBV Surface antigen Peptide of  HLA Class I- invention (SLP) SEQ ID class I Class I- C- BCI SLP SLP Start End Length Sequence^(A) NO: molecule B score^(B) score^(C) score^(D) SLP# Start End 175 182 8 MENITSGF 1146 B*4901 40 1,40 56 30 175 210 175 182 8 MENITSGF ″ B*5001 35 1,40 49 ″ ″ ″ 175 182 8 MENITSGF ″ B*1801 30 1,40 42 ″ ″ ″ 175 183 9 MENITSGFL 1147 B*4403 90 0,93 84 ″ ″ ″ 175 183 9 MENITSGFL ″ B*4402 85 0,93 79 ″ ″ ″ 175 183 9 MENITSGFL ″ B*4001 75 0,93 70 ″ ″ ″ 175 183 9 MENITSGFL ″ B*5001 25 0,93 23 ″ ″ ″ 175 183 9 MENITSGFL ″ B*4901 20 0,93 19 ″ ″ ″ 175 184 10 MENITSGFLG 1148 B*4402 75 0,59 44 ″ ″ ″ 175 184 10 MENITSGFLG ″ B*4403 60 0,59 35 ″ ″ ″ 175 185 11 MENITSGFLGP 1149 B*4402 35 0,19 7 ″ ″ ″ 175 186 12 MENITSGFLGPL 1150 B*4001 90 0,80 72 ″ ″ ″ 175 186 12 MENITSGFLGPL ″ B*4002 80 0,80 64 ″ ″ ″ 175 186 12 MENITSGFLGPL ″ B*4402 80 0,80 64 ″ ″ ″ 175 186 12 MENITSGFLGPL ″ B*4403 80 0,80 64 ″ ″ ″ 175 186 12 MENITSGFLGPL ″ B*1801 70 0,80 56 ″ ″ ″ 175 186 12 MENITSGFLGPL ″ B*3701 60 0,80 48 ″ ″ ″ 175 186 12 MENITSGFLGPL ″ B*5001 55 0,80 44 ″ ″ ″ 175 186 12 MENITSGFLGPL ″ B*4901 30 0,80 24 ″ ″ ″ 176 186 11 ENITSGFLGPL 1151 A*6802 20 0,80 16 ″ ″ ″ 175 187 13 MENITSGFLGPLL 1152 B*4402 95 0,77 73 ″ ″ ″ 175 187 13 MENITSGFLGPLL ″ B*4403 95 0,77 73 ″ ″ ″ 175 187 13 MENITSGFLGPLL ″ B*4001 85 0,77 66 ″ ″ ″ 175 187 13 MENITSGFLGPLL ″ B*5001 75 0,77 58 ″ ″ ″ 175 187 13 MENITSGFLGPLL ″ B*3701 70 0,77 54 ″ ″ ″ 175 187 13 MENITSGFLGPLL ″ B*4002 65 0,77 50 ″ ″ ″ 175 187 13 MENITSGFLGPLL ″ B*4901 60 0,77 46 ″ ″ ″ 175 187 13 MENITSGFLGPLL ″ B*1801 40 0,77 31 ″ ″ ″ 175 187 13 MENITSGFLGPLL ″ B*1301 25 0,77 19 ″ ″ ″ 178 187 10 ITSGFLGPLL 1153 A*3001 15 0,77 12 ″ ″ ″ 175 188 14 MENITSGFLGPLLV 1154 B*4901 95 1,48 141 ″ ″ ″ 175 188 14 MENITSGFLGPLLV ″ B*4402 90 1,48 133 ″ ″ ″ 175 188 14 MENITSGFLGPLLV ″ B*4403 85 1,48 126 ″ ″ ″ 175 188 14 MENITSGFLGPLLV ″ B*5001 80 1,48 119 ″ ″ ″ 175 188 14 MENITSGFLGPLLV ″ B*4001 65 1,48 96 ″ ″ ″ 175 188 14 MENITSGFLGPLLV ″ B*3701 50 1,48 74 ″ ″ ″ 175 188 14 MENITSGFLGPLLV ″ B*4002 10 1,48 15 ″ ″ ″ 182 193 12 FLGPLLVLQAGF 1155 B*1501 30 1,17 35 ″ ″ ″ 186 193 8 LLVLQAGF 1156 B*1501 10 1,17 12 ″ ″ ″ 187 194 8 LVLQAGFF 1157 A*2601 15 0,99 15 ″ ″ ″ 182 195 14 FLGPLLVLQAGFFL 1158 A*0201 63 1,59 100 ″ ″ ″ 182 195 14 FLGPLLVLQAGFFL ″ A*0206 55 1,59 87 ″ ″ ″ 186 195 10 LLVLqAGFFL 1159 A*0201 66 1,59 104 ″ ″ ″ 187 195 9 LVLQAGFFL 1160 A*0201 20 1,59 32 ″ ″ ″ 187 196 10 LVLQAGFFLL 1161 A*0206 20 1,85 37 ″ ″ ″ 188 196 9 VLQAGFFLL 1162 A*0201 26 1,85 48 ″ ″ ″ 189 196 8 LQAGFFLL 1163 B*3701 85 1,85 157 ″ ″ ″ 189 196 8 LQAGFFLL ″ B*4801 60 1,85 111 ″ ″ ″ 189 196 8 LQAGFFLL ″ B*1301 50 1,85 92 ″ ″ ″ 189 196 8 LQAGFFLL ″ B*3901 45 1,85 83 ″ ″ ″ 189 196 8 LQAGFFLL ″ B*1302 40 1,85 74 ″ ″ ″ 189 196 8 LQAGFFLL ″ B*3801 35 1,85 65 ″ ″ ″ 189 196 8 LQAGFFLL ″ B*5001 30 1,85 55 ″ ″ ″ 187 198 12 LVLQAGFFLLTR 1164 A*7401 30 1,36 41 ″ ″ ″ 187 198 12 LVLQAGFFLLTR ″ A*3101 10 1,36 14 ″ ″ ″ 187 198 12 LVLQAGFFLLTR ″ A*1101 5 1,36 7 ″ ″ ″ 188 198 11 VLQAGFFLLTR 1165 A*7401 90 1,36 122 ″ ″ ″ 189 198 10 LQAGFFLLTR 1166 A*3101 80 1,36 109 ″ ″ ″ 189 198 10 LQAGFFLLTR ″ A*7401 65 1,36 88 ″ ″ ″ 189 198 10 LQAGFFLLTR ″ A*1101 15 1,36 20 ″ ″ ″ 190 198 9 QAGFFLLTR 1167 A*7401 10 1,36 14 ″ ″ ″ 191 198 8 AGFFLLTR 1168 A*7401 70 1,36 95 ″ ″ ″ 189 199 11 LQAGFFLLTRI 1169 B*5201 95 1,36 129 ″ ″ ″ 189 199 11 LQAGFFLLTRI ″ B*1302 85 1,36 115 ″ ″ ″ 189 199 11 LQAGFFLLTRI ″ B*4901 50 1,36 68 ″ ″ ″ 189 199 11 LQAGFFLLTRI ″ B*1301 30 1,36 41 ″ ″ ″ 189 199 11 LQAGFFLLTRI ″ B*4001 25 1,36 34 ″ ″ ″ 189 199 11 LQAGFFLLTRI ″ B*5001 15 1,36 20 ″ ″ ″ 189 199 11 LQAGFFLLTRI ″ B*3701 10 1,36 14 ″ ″ ″ 189 200 12 LQAGFFLLTRIL 1170 B*4001 60 1,90 114 ″ ″ ″ 189 200 12 LQAGFFLLTRIL ″ B*3701 40 1,90 76 ″ ″ ″ 189 200 12 LQAGFFLLTRIL ″ B*4801 40 1,90 76 ″ ″ ″ 189 200 12 LQAGFFLLTRIL ″ B*3901 30 1,90 57 ″ ″ ″ 189 200 12 LQAGFFLLTRIL ″ B*5001 5 1,90 9 ″ ″ ″ 189 202 14 LQAGFFLLTRILTI 1171 B*5201 80 1,73 139 ″ ″ ″ 189 202 14 LQAGFFLLTRILTI ″ B*4901 65 1,73 113 ″ ″ ″ 189 202 14 LQAGFFLLTRILTI ″ B*5001 65 1,73 113 ″ ″ ″ 189 202 14 LQAGFFLLTRILTI ″ B*1301 60 1,73 104 ″ ″ ″ 189 202 14 LQAGFFLLTRILTI ″ B*1302 55 1,73 95 ″ ″ ″ 189 202 14 LQAGFFLLTRILTI ″ A*0206 50 1,73 87 ″ ″ ″ 189 202 14 LQAGFFLLTRILTI ″ B*3701 45 1,73 78 ″ ″ ″ 189 202 14 LQAGFFLLTRILTI ″ B*4001 45 1,73 78 ″ ″ ″ 191 202 12 AGFFLLTRILTI 1172 B*5201 50 1,73 87 ″ ″ ″ 194 202 9 FLLTRILTI 1173 B*0801 80 1,73 139 ″ ″ ″ 194 202 9 FLLTRILTI ″ A*0201 37 1,73 64 ″ ″ ″ 194 206 13 FLLTRILTIPQSL 1174 B*0801 100 1,23 123 ″ ″ ″ 194 206 13 FLLTRILTIPQSL ″ A*0201 29 1,23 35 ″ ″ ″ 195 206 12 LLTRILTIPQSL 1175 B*1402 70 1,23 86 ″ ″ ″ 196 206 11 LTRILTIPQSL 1176 A*3001 25 1,23 31 ″ ″ ″ 196 206 11 LTRILTIPQSL ″ B*1402 10 1,23 12 ″ ″ ″ 197 206 10 TRILTIPQSL 1177 B*3901 100 1,23 123 ″ ″ ″ 197 206 10 TRILTIPQSL ″ B*2705 5 1,23 6 ″ ″ ″ 196 209 14 LTRILTIPQSLDSW 1178 B*5701 75 1,47 111 ″ ″ ″ 196 209 14 LTRILTIPQSLDSW ″ B*5802 40 1,47 59 ″ ″ ″ 198 209 12 RILTIPQSLDSW 1179 B*5801 65 1,47 96 ″ ″ ″ 198 209 12 RILTIPQSLDSW ″ A*3201 60 1,47 88 ″ ″ ″ 198 209 12 RILTIPQSLDSW ″ B*5701 50 1,47 74 ″ ″ ″ 200 209 10 LTIPQSLDSW 1180 B*5802 90 1,47 133 ″ ″ ″ 200 209 10 LTIPQSLDSW ″ A*2501 40 1,47 59 ″ ″ ″ 197 210 14 TRILTIPQSLDSWW 1181 B*4402 20 0,79 16 ″ ″ ″ 197 210 14 TRILTIPQSLDSWW ″ B*4403 15 0,79 12 ″ ″ ″ 198 210 13 RILTIPQSLDSWW 1182 B*5801 60 0,79 47 ″ ″ ″ 198 210 13 RILTIPQSLDSWW ″ B*5701 40 0,79 31 ″ ″ ″ 200 210 11 LTIPQSLDSWW 1183 B*5802 75 0,79 59 ″ ″ ″ 200 210 11 LTIPQSLDSWW ″ B*5801 40 0,79 31 ″ ″ ″ 202 210 9 IPQSLDSWW 1184 B*5301 50 0,79 39 ″ ″ ″ Cumulative Class I-BCI 6882 score: 239 246 8 CPPICPGY 1185 B*3501 45 1,44 65 31 239 274 239 248 10 CPPICPGYRW 1186 B*5301 85 1,94 165 ″ ″ ″ 240 251 12 PPICPGYRWMCL 1187 B*3503 50 1,46 73 ″ ″ ″ 243 251 9 CPGYRWMCL 1188 B*0801 75 1,46 110 ″ ″ ″ 243 251 9 CPGYRWMCL ″ B*1402 50 1,46 73 ″ ″ ″ 243 252 10 CPGYRWMCLR 1189 A*3303 5 1,04 5 ″ ″ ″ 244 252 9 PGYRWMCLR 1190 A*3101 5 1,04 5 ″ ″ ″ 245 252 8 GYRWMCLR 1191 A*3101 95 1,04 99 ″ ″ ″ 245 252 8 GYRWMCLR ″ A*3303 10 1,04 10 ″ ″ ″ 245 253 9 GYRWMCLRR 1192 A*3101 45 0,95 43 ″ ″ ″ 245 254 10 GYRWMCLRRF 1193 A*2402 10 1,01 10 ″ ″ ″ 246 254 9 YRWMCLRRF 1194 B*2702 40 1,01 41 ″ ″ ″ 246 254 9 YRWMCLRRF ″ B*2705 40 1,01 41 ″ ″ ″ 245 255 11 GYRWMCLRRFI 1195 A*3001 35 0,99 35 ″ ″ ″ 246 255 10 YRWMCLRRFI 1196 B*1402 90 0,99 89 ″ ″ ″ 246 255 10 YRWMCLRRFI ″ B*2702 85 0,99 84 ″ ″ ″ 246 255 10 YRWMCLRRFI ″ B*2705 20 0,99 20 ″ ″ ″ 243 256 14 CPGYRWMCLRRFII 1197 B*0801 65 0,86 56 ″ ″ ″ 243 256 14 CPGYRWMCLRRFII ″ B*5101 25 0,86 21 ″ ″ ″ 246 256 11 YRWMCLRRFII 1198 B*2702 100 0,86 86 ″ ″ ″ 246 256 11 YRWMCLRRFII ″ B*1402 75 0,86 64 ″ ″ ″ 246 256 11 YRWMCLRRFII ″ B*2705 65 0,86 56 ″ ″ ″ 246 256 11 YRWMCLRRFII ″ B*3801 60 0,86 51 ″ ″ ″ 247 256 10 RWMCLRRFII 1199 A*2402 55 0,86 47 ″ ″ ″ 247 256 10 RWMCLRRFII ″ A*2301 35 0,86 30 ″ ″ ″ 245 257 13 GYRWMCLRRFIIF 1200 A*2301 85 1,08 92 ″ ″ ″ 246 257 12 YRWMCLRRFIIF 1201 B*1402 100 1,08 108 ″ ″ ″ 246 257 12 YRWMCLRRFIIF ″ B*2702 75 1,08 81 ″ ″ ″ 246 257 12 YRWMCLRRFIIF ″ B*2705 60 1,08 65 ″ ″ ″ 247 257 11 RWMCLRRFIIF 1202 A*2402 50 1,08 54 ″ ″ ″ 249 257 9 MCLRRFIIF 1203 B*0801 55 1,08 59 ″ ″ ″ 245 258 14 GYRWMCLRRFIIFL 1204 A*3001 45 1,61 72 ″ ″ ″ 246 258 13 YRWMCLRRFIIFL 1205 B*1402 95 1,61 153 ″ ″ ″ 246 258 13 YRWMCLRRFIIFL ″ B*2705 85 1,61 137 ″ ″ ″ 246 258 13 YRWMCLRRFIIFL ″ B*2702 60 1,61 96 ″ ″ ″ 246 258 13 YRWMCLRRFIIFL ″ B*3801 20 1,61 32 ″ ″ ″ 249 258 10 MCLRRFIIFL 1206 B*0801 15 1,61 24 ″ ″ ″ 251 258 8 LRRFIIFL 1207 B*1402 60 1,61 96 ″ ″ ″ 246 259 14 YRWMCLRRFIIFLF 1208 B*2702 55 1,73 95 ″ ″ ″ 246 259 14 YRWMCLRRFIIFLF ″ B*2705 45 1,73 78 ″ ″ ″ 246 259 14 YRWMCLRRFIIFLF ″ B*3801 40 1,73 69 ″ ″ ″ 247 259 13 RWMCLRRFIIFLF 1209 A*2402 100 1,73 173 ″ ″ ″ 247 259 13 RWMCLRRFIIFLF ″ A*2301 80 1,73 138 ″ ″ ″ 249 259 11 MCLRRFIIFLF 1210 B*1801 50 1,73 86 ″ ″ ″ 251 259 9 LRRFIIFLF 1211 B*2705 25 1,73 43 ″ ″ ″ 252 259 8 RRFIIFLF 1212 B*2702 90 1,73 155 ″ ″ ″ 252 259 8 RRFIIFLF ″ B*2705 70 1,73 121 ″ ″ ″ 252 259 8 RRFIIFLF ″ B*3801 70 1,73 121 ″ ″ ″ 247 260 14 RWMCLRRFIIFLFI 1213 A*2402 65 1,60 104 ″ ″ ″ 248 260 13 WMCLRRFIIFLFI 1214 B*0801 5 1,60 8 ″ ″ ″ 249 260 12 MCLRRFIIFLFI 1215 B*0801 90 1,60 144 ″ ″ ″ 250 260 11 CLRRFIIFLFI 1216 A*3001 60 1,60 96 ″ ″ ″ 251 260 10 LRRFIIFLFI 1217 B*1402 25 1,60 40 ″ ″ ″ 252 260 9 RRFIIFLFI 1218 B*2705 75 1,60 120 ″ ″ ″ 252 260 9 RRFIIFLFI ″ B*3801 50 1,60 80 ″ ″ ″ 252 260 9 RRFIIFLFI ″ B*2702 35 1,60 56 ″ ″ ″ 248 261 14 WMCLRRFIIFLFIL 1219 B*0801 20 1,79 36 ″ ″ ″ 249 261 13 MCLRRFIIFLFIL 1220 B*0801 70 1,79 126 ″ ″ ″ 250 261 12 CLRRFIIFLFIL 1221 B*0801 25 1,79 45 ″ ″ ″ 251 261 11 LRRFIIFLFIL 1222 B*1402 35 1,79 63 ″ ″ ″ 252 261 10 RRFIIFLFIL 1223 B*2705 100 1,79 179 ″ ″ ″ 252 261 10 RRFIIFLFIL ″ B*3801 85 1,79 152 ″ ″ ″ 252 261 10 RRFIIFLFIL ″ B*2702 80 1,79 144 ″ ″ ″ 252 261 10 RRFIIFLFIL ″ B*4801 50 1,79 90 ″ ″ ″ 252 261 10 RRFIIFLFIL ″ B*4001 10 1,79 18 ″ ″ ″ 252 261 10 RRFIIFLFIL ″ B*4002 5 1,79 9 ″ ″ ″ 253 261 9 RFIIFLFIL 1224 B*4001 15 1,79 27 ″ ″ ″ 254 261 8 FIIFLFIL 1225 A*2501 10 1,79 18 ″ ″ ″ 249 262 14 MCLRRFIIFLFILL 1226 B*0801 60 1,50 90 ″ ″ ″ 250 262 13 CLRRFIIFLFILL 1227 A*3001 5 1,50 7 ″ ″ ″ 251 262 12 LRRFIIFLFILL 1228 B*2705 35 1,50 52 ″ ″ ″ 251 262 12 LRRFIIFLFILL ″ B*1402 5 1,50 7 ″ ″ ″ 252 262 11 RRFIIFLFILL 1229 B*2702 95 1,50 142 ″ ″ ″ 252 262 11 RRFIIFLFILL ″ B*2705 95 1,50 142 ″ ″ ″ 252 262 11 RRFIIFLFILL ″ B*3801 80 1,50 120 ″ ″ ″ 252 262 11 RRFIIFLFILL ″ B*4002 60 1,50 90 ″ ″ ″ 252 262 11 RRFIIFLFILL ″ B*4801 45 1,50 67 ″ ″ ″ 253 262 10 RFIIFLFILL 1230 B*4001 20 1,50 30 ″ ″ ″ 254 262 9 FIIFLFILL 1231 A*6802 60 1,50 90 ″ ″ ″ 254 262 9 FIIFLFILL ″ A*2601 30 1,50 45 ″ ″ ″ 251 263 13 LRRFIIFLFILLL 1232 B*2705 50 1,90 95 ″ ″ ″ 252 263 12 RRFIIFLFILLL 1233 B*2705 90 1,90 171 ″ ″ ″ 252 263 12 RRFIIFLFILLL ″ B*3801 90 1,90 171 ″ ″ ″ 252 263 12 RRFIIFLFILLL ″ B*2702 70 1,90 133 ″ ″ ″ 252 263 12 RRFIIFLFILLL ″ B*4002 40 1,90 76 ″ ″ ″ 252 263 12 RRFIIFLFILLL ″ B*4801 5 1,90 10 ″ ″ ″ 254 263 10 FIIFLFILLL 1234 A*2601 65 1,90 124 ″ ″ ″ 252 264 13 RRFIIFLFILLLC 1235 B*2705 30 0,75 22 ″ ″ ″ 252 265 14 RRFIIFLFILLLCL 1236 B*2705 80 1,60 128 ″ ″ ″ 252 265 14 RRFIIFLFILLLCL ″ B*2702 50 1,60 80 ″ ″ ″ 252 265 14 RRFIIFLFILLLCL ″ B*4002 25 1,60 40 ″ ″ ″ 252 265 14 RRFIIFLFILLLCL ″ B*3801 10 1,60 16 ″ ″ ″ 257 265 9 FLFILLLCL 1237 A*0201 60 1,60 96 ″ ″ ″ 254 266 13 FIIFLFILLLCLI 1238 A*6802 40 0,76 30 ″ ″ ″ 257 266 10 FLFIlLLCLI 1239 A*0201 31 0,76 24 ″ ″ ″ 257 266 10 FLFILLLCLI ″ B*5101 15 0,76 11 ″ ″ ″ 254 267 14 FIIFLFILLLCLIF 1240 A*2501 80 1,24 99 ″ ″ ″ 254 267 14 FIIFLFILLLCLIF ″ A*2601 70 1,24 86 ″ ″ ″ 254 267 14 FIIFLFILLLCLIF ″ B*1501 50 1,24 62 ″ ″ ″ 254 267 14 FIIFLFILLLCLIF ″ B*4601 35 1,24 43 ″ ″ ″ 254 267 14 FIIFLFILLLCLIF ″ A*2902 20 1,24 25 ″ ″ ″ 255 267 13 IIFLFILLLCLIF 1241 A*3201 20 1,24 25 ″ ″ ″ 256 267 12 IFLFILLLCLIF 1242 A*2301 95 1,24 117 ″ ″ ″ 256 267 12 IFLFILLLCLIF ″ A*2902 30 1,24 37 ″ ″ ″ 257 267 11 FLFILLLCLIF 1243 B*4601 80 1,24 99 ″ ″ ″ 257 267 11 FLFILLLCLIF ″ B*1501 65 1,24 80 ″ ″ ″ 257 267 11 FLFILLLCLIF ″ B*1502 65 1,24 80 ″ ″ ″ 258 267 10 LFILLLCLIF 1244 A*2301 50 1,24 62 ″ ″ ″ 256 268 13 IFLFILLLCLIFL 1245 A*2301 10 1,44 14 ″ ″ ″ 257 268 12 FLFILLLCLIFL 1246 A*0201 40 1,44 57 ″ ″ ″ 259 268 10 FILL1CLIFL 1247 A*0201 49 1,44 70 ″ ″ ″ 259 268 10 FILLLCLIFL ″ A*0206 5 1,44 7 ″ ″ ″ 260 268 9 ILLLCLIFL 1248 A*0201 71 1,44 103 ″ ″ ″ 256 269 14 IFLFILLLCLIFLL 1249 A*2301 65 1,83 119 ″ ″ ″ 257 269 13 FLFILLLCLIFLL 1250 A*0201 23 1,83 42 ″ ″ ″ 260 269 10 ILLLcLIFLL 1251 A*0201 77 1,83 141 ″ ″ ″ 261 269 9 LLLCLIFLL 1252 A*0201 83 1,83 152 ″ ″ ″ 259 270 12 FILLLCLIFLLV 1253 A*0206 40 1,71 68 ″ ″ ″ 260 270 11 ILLLCLIFLLV 1254 A*0206 45 1,71 77 ″ ″ ″ 261 270 10 LLLCLIFLLV 1255 A*0206 65 1,71 111 ″ ″ ″ 261 270 10 LLLC1IFLLV ″ A*0201 54 1,71 93 ″ ″ ″ 262 270 9 LLCLIFLLV 1256 A*0201 6 1,71 10 ″ ″ ″ 261 271 11 LLLCLIFLLVL 1257 A*0206 85 1,61 136 ″ ″ ″ 261 274 14 LLLCLIFLLVLLDY 1258 A*2902 80 1,83 147 ″ ″ ″ 262 274 13 LLCLIFLLVLLDY 1259 A*2902 90 1,83 165 ″ ″ ″ 262 274 13 LLCLIFLLVLLDY ″ A*0101 75 1,83 138 ″ ″ ″ 264 274 11 CLIFLLVLLDY 1260 A*0101 85 1,83 156 ″ ″ ″ 265 274 10 LIFLLVLLDY 1261 A*0101 55 1,83 101 ″ ″ ″ 265 274 10 LIFLLVLLDY ″ A*0301 35 1,83 64 ″ ″ ″ 266 274 9 IFLLVLLDY 1262 A*2902 70 1,83 128 ″ ″ ″ 267 274 8 FLLVLLDY 1263 B*1502 60 1,83 110 ″ ″ ″ Cumulative Class I-BCI 10214 score: 324 331 8 IPIPSSWA 1264 B*5601 85 0,15 13 ″ ″ ″ 324 331 8 IPIPSSWA ″ B*5501 55 0,16 9 ″ ″ ″ 324 332 9 IPIPSSWAF 1265 B*3501 70 1,87 131 ″ ″ ″ 324 332 9 IPIPSSWAF ″ B*3503 55 1,87 103 ″ ″ ″ 324 332 9 IPIPSSWAF ″ B*5301 45 1,87 84 ″ ″ ″ 324 333 10 IPIPSSWAFA 1266 B*5601 100 1,02 102 ″ ″ ″ 324 333 10 IPIPSSWAFA ″ B*5501 85 1,02 87 ″ ″ ″ 326 333 8 IPSSWAFA 1267 B*5601 45 1,02 46 ″ ″ ″ 326 333 8 IPSSWAFA ″ B*5501 40 1,02 41 ″ ″ ″ 323 334 12 CIPIPSSWAFAK 1268 A*0301 80 1,04 83 ″ ″ ″ 323 334 12 CIPIPSSWAFAK ″ A*1101 30 1,04 31 ″ ″ ″ 324 334 11 IPIPSSWAFAK 1269 B*3501 15 1,04 16 ″ ″ ″ 326 334 9 IPSSWAFAK 1270 A*1101 10 1,04 10 ″ ″ ″ 327 334 8 PSSWAFAK 1271 A*0301 45 1,04 47 ″ ″ ″ 324 335 12 IPIPSSWAFAKY 1272 B*3503 85 1,90 161 ″ ″ ″ 324 335 12 IPIPSSWAFAKY ″ B*3501 80 1,90 152 ″ ″ ″ 324 335 12 IPIPSSWAFAKY ″ B*5301 25 1,90 47 ″ ″ ″ 325 335 11 PIPSSWAFAKY 1273 A*2501 30 1,90 57 ″ ″ ″ 326 335 10 IPSSWAFAKY 1274 B*3501 35 1,90 66 ″ ″ ″ 327 335 9 PSSWAFAKY 1275 A*0101 65 1,90 123 ″ ″ ″ 327 335 9 PSSWAFAKY ″ A*3002 45 1,90 85 ″ ″ ″ 328 335 8 SSWAFAKY 1276 A*2501 75 1,90 142 ″ ″ ″ 328 335 8 SSWAFAKY ″ A*3002 75 1,90 142 ″ ″ ″ 328 335 8 SSWAFAKY ″ A*2902 55 1,90 104 ″ ″ ″ 324 336 13 IPIPSSWAFAKYL 1277 B*3503 80 1,06 85 ″ ″ ″ 324 336 13 IPIPSSWAFAKYL ″ B*5101 65 1,06 69 ″ ″ ″ 324 337 14 IPIPSSWAFAKYLW 1278 B*5301 55 1,58 87 ″ ″ ″ 324 337 14 IPIPSSWAFAKYLW ″ B*5101 20 1,58 32 ″ ″ ″ 324 337 14 IPIPSSWAFAKYLW ″ B*5701 5 1,58 8 ″ ″ ″ 326 337 12 IPSSWAFAKYLW 1279 B*5301 100 1,58 158 ″ ″ ″ 326 337 12 IPSSWAFAKYLW ″ B*5802 10 1,58 16 ″ ″ ″ 328 337 10 SSWAFAKYLW 1280 B*5802 100 1,58 158 ″ ″ ″ 328 337 10 SSWAFAKYLW ″ B*5701 95 1,58 150 ″ ″ ″ 328 337 10 SSWAFAKYLW ″ B*4403 45 1,58 71 ″ ″ ″ 328 337 10 SSWAFAKYLW ″ B*5801 35 1,58 55 ″ ″ ″ 328 337 10 SSWAFAKYLW ″ B*4402 15 1,58 24 ″ ″ ″ 330 337 8 WAFAKYLW 1281 B*5801 85 1,58 134 ″ ″ ″ 330 337 8 WAFAKYLW ″ B*5701 65 1,58 103 ″ ″ ″ 330 337 8 WAFAKYLW ″ B*5802 50 1,58 79 ″ ″ ″ 326 339 14 IPSSWAFAKYLWEW 1282 B*5301 95 1,83 174 ″ ″ ″ 328 339 12 SSWAFAKYLWEW 1283 B*5701 100 1,83 183 ″ ″ ″ 328 339 12 SSWAFAKYLWEW ″ B*5801 95 1,83 174 ″ ″ ″ 328 339 12 SSWAFAKYLWEW ″ B*5802 65 1,83 119 ″ ″ ″ 328 339 12 SSWAFAKYLWEW ″ A*3201 55 1,83 101 ″ ″ ″ 328 339 12 SSWAFAKYLWEW ″ B*4403 50 1,83 91 ″ ″ ″ 328 339 12 SSWAFAKYLWEW ″ B*4402 10 1,83 18 ″ ″ ″ 330 339 10 WAFAKYLWEW 1284 B*5802 85 1,83 156 ″ ″ ″ 330 339 10 WAFAKYLWEW ″ B*5201 70 1,83 128 ″ ″ ″ 331 339 9 AFAKYLWEW 1285 B*4402 50 1,83 91 ″ ″ ″ 331 339 9 AFAKYLWEW ″ B*4403 40 1,83 73 ″ ″ ″ 332 339 8 FAKYLWEW 1286 B*4601 40 1,83 73 ″ ″ ″ 332 339 8 FAKYLWEW ″ B*5701 30 1,83 55 ″ ″ ″ 330 342 13 WAFAKYLWEWASV 1287 A*6802 85 1,92 164 ″ ″ ″ 330 342 13 WAFAKYLWEWASV ″ B*1402 20 1,92 38 ″ ″ ″ 332 342 11 FAKYLWEWASV 1288 B*4601 50 1,92 96 ″ ″ ″ 330 343 14 WAFAKYLWEWASVR 1289 A*3303 80 1,07 85 ″ ″ ″ 330 343 14 WAFAKYLWEWASVR ″ A*6801 50 1,07 53 ″ ″ ″ 330 343 14 WAFAKYLWEWASVR ″ A*7401 15 1,07 16 ″ ″ ″ 331 343 13 AFAKYLWEWASVR 1290 A*3101 70 1,07 75 ″ ″ ″ 331 343 13 AFAKYLWEWASVR ″ A*3303 35 1,07 37 ″ ″ ″ 332 343 12 FAKYLWEWASVR 1291 A*3303 85 1,07 91 ″ ″ ″ 332 343 12 FAKYLWEWASVR ″ A*6801 60 1,07 64 ″ ″ ″ 332 343 12 FAKYLWEWASVR ″ A*3101 55 1,07 59 ″ ″ ″ 334 343 10 KYLWEWASVR 1292 A*3101 100 1,07 107 ″ ″ ″ 335 343 9 YLWEWASVR 1293 A*7401 85 1,07 91 ″ ″ ″ 335 343 9 YLWEWASVR ″ A*3303 40 1,07 43 ″ ″ ″ 335 343 9 YLWEWASVR ″ A*3101 35 1,07 37 ″ ″ ″ 335 343 9 YLWEWASVR ″ A*0301 20 1,07 21 ″ ″ ″ 331 344 14 AFAKYLWEWASVRF 1294 A*2402 30 1,86 56 ″ ″ ″ 331 344 14 AFAKYLWEWASVRF ″ A*2301 5 1,86 9 ″ ″ ″ 332 344 13 FAKYLWEWASVRF 1295 B*4601 75 1,86 139 ″ ″ ″ 335 344 10 YLWEWASVRF 1296 B*1502 90 1,86 167 ″ ″ ″ 335 344 10 YLWEWASVRF ″ B*1525 45 1,86 84 ″ ″ ″ 337 344 8 WEWASVRF 1297 B*3701 80 1,86 149 ″ ″ ″ 337 344 8 WEWASVRF ″ B*4901 80 1,86 149 ″ ″ ″ 337 344 8 WEWASVRF ″ B*5001 50 1,86 93 ″ ″ ″ 337 344 8 WEWASVRF ″ B*1301 45 1,86 84 ″ ″ ″ 337 344 8 WEWASVRF ″ B*4403 5 1,86 9 ″ ″ ″ 337 345 9 WEWASVRFS 1298 B*4403 65 0,50 33 ″ ″ ″ 337 345 9 WEWASVRFS ″ B*5001 60 0,50 30 ″ ″ ″ 337 345 9 WEWASVRFS ″ B*4002 55 0,50 28 ″ ″ ″ 337 345 9 WEWASVRFS ″ B*4901 15 0,50 8 ″ ″ ″ 333 346 14 AKYLWEWASVRFSW 1299 B*4403 35 1,50 52 ″ ″ ″ 334 346 13 KYLWEWASVRFSW 1300 A*2402 95 1,50 142 ″ ″ ″ 334 346 13 KYLWEWASVRFSW ″ A*2301 75 1,50 112 ″ ″ ″ 335 346 12 YLWEWASVRFSW 1301 A*3201 80 1,50 120 ″ ″ ″ 335 346 12 YLWEWASVRFSW ″ B*1302 75 1,50 112 ″ ″ ″ 335 346 12 YLWEWASVRFSW ″ B*5201 45 1,50 67 ″ ″ ″ 337 346 10 WEWASVRFSW 1302 B*1301 100 1,50 150 ″ ″ ″ 337 346 10 WEWASVRFSW ″ B*4402 100 1,50 150 ″ ″ ″ 337 346 10 WEWASVRFSW ″ B*4403 100 1,50 150 ″ ″ ″ 337 346 10 WEWASVRFSW ″ B*1302 90 1,50 135 ″ ″ ″ 337 346 10 WEWASVRFSW ″ B*4002 90 1,50 135 ″ ″ ″ 337 346 10 WEWASVRFSW ″ B*4901 75 1,50 112 ″ ″ ″ 339 346 8 WASVRFSW 1303 B*5801 50 1,50 75 ″ ″ ″ 334 347 14 KYLWEWASVRFSWL 1304 A*2402 90 1,37 123 ″ ″ ″ 334 347 14 KYLWEWASVRFSWL ″ A*2301 40 1,37 55 ″ ″ ″ 335 347 13 YLWEWASVRFSWL 1305 A*0201 100 1,37 137 ″ ″ ″ 335 347 13 YLWEWASVRFSWL ″ A*0206 60 1,37 82 ″ ″ ″ 337 347 11 WEWASVRFSWL 1306 B*4001 95 1,37 130 ″ ″ ″ 337 347 11 WEWASVRFSWL ″ B*3701 90 1,37 123 ″ ″ ″ 337 347 11 WEWASVRFSWL ″ B*5001 90 1,37 123 ″ ″ ″ 337 347 11 WEWASVRFSWL ″ B*4002 85 1,37 117 ″ ″ ″ 337 347 11 WEWASVRFSWL ″ B*4901 85 1,37 117 ″ ″ ″ 337 347 11 WEWASVRFSWL ″ B*1301 80 1,37 110 ″ ″ ″ 337 347 11 WEWASVRFSWL ″ B*4402 55 1,37 75 ″ ″ ″ 337 347 11 WEWASVRFSWL ″ B*1302 10 1,37 14 ″ ″ ″ 339 347 9 WASVRFSWL 1307 B*0801 50 1,37 69 ″ ″ ″ 337 348 12 WEWASVRFSWLS 1308 B*1801 80 0,54 43 ″ ″ ″ 337 348 12 WEWASVRFSWLS ″ B*4002 70 0,54 38 ″ ″ ″ 337 348 12 WEWASVRFSWLS ″ B*4901 45 0,54 24 ″ ″ ″ 337 348 12 WEWASVRFSWLS ″ B*5001 45 0,54 24 ″ ″ ″ 337 348 12 WEWASVRFSWLS ″ B*4403 20 0,54 11 ″ ″ ″ 337 348 12 WEWASVRFSWLS ″ B*3701 5 0,54 3 ″ ″ ″ 341 348 8 SVRFSWLS 1309 A*3001 40 0,54 22 ″ ″ ″ 337 349 13 WEWASVRFSWLSL 1310 B*1801 100 1,61 161 ″ ″ ″ 337 349 13 WEWASVRFSWLSL ″ B*3701 100 1,61 161 ″ ″ ″ 337 349 13 WEWASVRFSWLSL ″ B*4001 100 1,61 161 ″ ″ ″ 337 349 13 WEWASVRFSWLSL ″ B*4002 100 1,61 161 ″ ″ ″ 337 349 13 WEWASVRFSWLSL ″ B*4901 100 1,61 161 ″ ″ ″ 337 349 13 WEWASVRFSWLSL ″ B*5001 100 1,61 161 ″ ″ ″ 337 349 13 WEWASVRFSWLSL ″ B*1301 90 1,61 145 ″ ″ ″ 337 349 13 WEWASVRFSWLSL ″ B*4403 75 1,61 120 ″ ″ ″ 337 349 13 WEWASVRFSWLSL ″ B*4402 70 1,61 112 ″ ″ ″ 339 349 11 WASVRFSWLSL 1311 B*1402 85 1,61 137 ″ ″ ″ 341 349 9 SVRFSWLSL 1312 A*3001 90 1,61 145 ″ ″ ″ 341 349 9 SVRFSWLSL ″ B*0702 80 1,61 129 ″ ″ ″ 342 349 8 VRFSWLSL 1313 B*3901 70 1,61 112 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL 1314 B*3701 95 1,15 109 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*4002 95 1,15 109 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*5001 95 1,15 109 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*1801 90 1,15 104 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*4901 90 1,15 104 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*1301 85 1,15 98 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*4001 80 1,15 92 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*4403 70 1,15 81 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*4801 70 1,15 81 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*4402 60 1,15 69 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*1302 50 1,15 58 ″ ″ ″ 342 350 9 VRFSWLSLL 1315 B*3801 65 1,15 75 ″ ″ ″ 342 350 9 VRFSWLSLL ″ B*2702 20 1,15 23 ″ ″ ″ 339 351 13 WASVRFSWLSLLV 1316 B*5101 30 1,47 44 ″ ″ ″ 341 351 11 SVRFSWLSLLV 1317 A*3001 85 1,47 125 ″ ″ ″ 340 353 14 ASVRFSWLSLLVPF 1318 B*4601 30 0,19 6 ″ ″ ″ 340 353 14 ASVRFSWLSLLVPF ″ B*1525 15 0,19 3 ″ ″ ″ 341 353 13 SVRFSWLSLLVPF 1319 B*1501 80 0,19 15 ″ ″ ″ 341 353 13 SVRFSWLSLLVPF ″ B*1525 60 0,19 11 ″ ″ ″ 341 353 13 SVRFSWLSLLVPF ″ B*1502 25 0,19 5 ″ ″ ″ 341 353 13 SVRFSWLSLLVPF ″ A*3001 20 0,19 4 ″ ″ ″ 342 353 12 VRFSWLSLLVPF 1320 B*2702 65 0,19 12 ″ ″ ″ 342 353 12 VRFSWLSLLVPF ″ B*2705 55 0,19 10 ″ ″ ″ 343 353 11 RFSWLSLLVPF 1321 A*3201 85 0,19 16 ″ ″ ″ 343 353 11 RFSWLSLLVPF ″ A*2402 80 0,19 15 ″ ″ ″ 344 353 10 FSWLSLLVPF 1322 B*4601 100 0,19 19 ″ ″ ″ 344 353 10 FSWLSLLVPF ″ B*1525 55 0,19 10 ″ ″ ″ 346 353 8 WLSLLVPF 1323 B*1502 10 0,19 2 ″ ″ ″ 341 354 14 SVRFSWLSLLVPFV 1324 A*3001 95 1,30 124 ″ ″ ″ 342 354 13 VRFSWLSLLVPFV 1325 B*2705 15 1,30 20 ″ ″ ″ 346 354 9 WLSLLVPFV 1326 A*0201 94 1,30 123 ″ ″ ″ 343 356 14 RFSWLSLLVPFVQW 1327 A*2402 25 1,92 48 ″ ″ ″ 344 356 13 FSWLSLLVPFVQW 1328 B*5801 90 1,92 173 ″ ″ ″ 344 356 13 FSWLSLLVPFVQW ″ B*5701 85 1,92 163 ″ ″ ″ 344 356 13 FSWLSLLVPFVQW ″ B*5802 60 1,92 115 ″ ″ ″ 344 356 13 FSWLSLLVPFVQW ″ B*5201 40 1,92 77 ″ ″ ″ 347 356 10 LSLLVPFVQW 1329 B*5802 80 1,92 154 ″ ″ ″ 344 357 14 FSWLSLLVPFVQWF 1330 B*4601 65 1,38 89 ″ ″ ″ 345 357 13 SWLSLLVPFVQWF 1331 A*2301 45 1,38 62 ″ ″ ″ 345 357 13 SWLSLLVPFVQWF ″ A*2402 35 1,38 48 ″ ″ ″ 347 357 11 LSLLVPFVQWF 1332 B*5802 20 1,38 28 ″ ″ ″ 348 357 10 SLLVPFVQWF 1333 B*1502 50 1,38 69 ″ ″ ″ 349 357 9 LLVPFVQWF 1334 B*1501 45 1,38 62 ″ ″ ″ 349 357 9 LLVPFVQWF ″ B*1525 10 1,38 14 ″ ″ ″ 346 358 13 WLSLLVPFVQWFV 1335 A*0201 80 1,65 132 ″ ″ ″ 346 358 13 WLSLLVPFVQWFV ″ A*0206 25 1,65 41 ″ ″ ″ 349 358 10 LLVPfVQWFV 1336 A*0201 97 1,65 161 ″ ″ ″ 349 358 10 LLVPFVQWFV ″ A*0206 90 1,65 149 ″ ″ ″ 350 358 9 LVPFVQWFV 1337 A*6802 100 1,65 165 ″ ″ ″ 350 358 9 LVPFVQWFV ″ A*0201 43 1,65 71 ″ ″ ″ Cumulative Class I-BCI 14976 score: 327 334 8 PSSWAFAK 1271 A*0301 45 1,04 47 33 323 358 327 335 9 PSSWAFAKY 1275 A*0101 65 1,90 123 ″ ″ ″ 327 335 9 PSSWAFAKY ″ A*3002 45 1,90 85 ″ ″ ″ 328 335 8 SSWAFAKY 1276 A*2501 75 1,90 142 ″ ″ ″ 328 335 8 SSWAFAKY ″ A*3002 75 1,90 142 ″ ″ ″ 328 335 8 SSWAFAKY ″ A*2902 55 1,90 104 ″ ″ ″ 328 337 10 SSWAFAKYLW 1280 B*5802 100 1,58 158 ″ ″ ″ 328 337 10 SSWAFAKYLW ″ B*5701 95 1,58 150 ″ ″ ″ 328 337 10 SSWAFAKYLW ″ B*4403 45 1,58 71 ″ ″ ″ 328 337 10 SSWAFAKYLW ″ B*5801 35 1,58 55 ″ ″ ″ 328 337 10 SSWAFAKYLW ″ B*4402 15 1,58 24 ″ ″ ″ 330 337 8 WAFAKYLW 1281 B*5801 85 1,58 134 ″ ″ ″ 330 337 8 WAFAKYLW ″ B*5701 65 1,58 103 ″ ″ ″ 330 337 8 WAFAKYLW ″ B*5802 50 1,58 79 ″ ″ ″ 328 339 12 SSWAFAKYLWEW 1283 B*5701 100 1,83 183 ″ ″ ″ 328 339 12 SSWAFAKYLWEW ″ B*5801 95 1,83 174 ″ ″ ″ 328 339 12 SSWAFAKYLWEW ″ B*5802 65 1,83 119 ″ ″ ″ 328 339 12 SSWAFAKYLWEW ″ A*3201 55 1,83 101 ″ ″ ″ 328 339 12 SSWAFAKYLWEW ″ B*4403 50 1,83 91 ″ ″ ″ 328 339 12 SSWAFAKYLWEW ″ B*4402 10 1,83 18 ″ ″ ″ 330 339 10 WAFAKYLWEW 1284 B*5802 85 1,83 156 ″ ″ ″ 330 339 10 WAFAKYLWEW ″ B*5201 70 1,83 128 ″ ″ ″ 331 339 9 AFAKYLWEW 1285 B*4402 50 1,83 91 ″ ″ ″ 331 339 9 AFAKYLWEW ″ B*4403 40 1,83 73 ″ ″ ″ 332 339 8 FAKYLWEW 1286 B*4601 40 1,83 73 ″ ″ ″ 332 339 8 FAKYLWEW ″ B*5701 30 1,83 55 ″ ″ ″ 330 342 13 WAFAKYLWEWASV 1287 A*6802 85 1,92 164 ″ ″ ″ 330 342 13 WAFAKYLWEWASV ″ B*1402 20 1,92 38 ″ ″ ″ 332 342 11 FAKYLWEWASV 1288 B*4601 50 1,92 96 ″ ″ ″ 330 343 14 WAFAKYLWEWASVR 1289 A*3303 80 1,07 85 ″ ″ ″ 330 343 14 WAFAKYLWEWASVR ″ A*6801 50 1,07 53 ″ ″ ″ 330 343 14 WAFAKYLWEWASVR ″ A*7401 15 1,07 16 ″ ″ ″ 331 343 13 AFAKYLWEWASVR 1290 A*3101 70 1,07 75 ″ ″ ″ 331 343 13 AFAKYLWEWASVR ″ A*3303 35 1,07 37 ″ ″ ″ 332 343 12 FAKYLWEWASVR 1291 A*3303 85 1,07 91 ″ ″ ″ 332 343 12 FAKYLWEWASVR ″ A*6801 60 1,07 64 ″ ″ ″ 332 343 12 FAKYLWEWASVR ″ A*3101 55 1,07 59 ″ ″ ″ 334 343 10 KYLWEWASVR 1292 A*3101 100 1,07 107 ″ ″ ″ 335 343 9 YLWEWASVR 1293 A*7401 85 1,07 91 ″ ″ ″ 335 343 9 YLWEWASVR ″ A*3303 40 1,07 43 ″ ″ ″ 335 343 9 YLWEWASVR ″ A*3101 35 1,07 37 ″ ″ ″ 335 343 9 YLWEWASVR ″ A*0301 20 1,07 21 ″ ″ ″ 331 344 14 AFAKYLWEWASVRF 1294 A*2402 30 1,86 56 ″ ″ ″ 331 344 14 AFAKYLWEWASVRF ″ A*2301 5 1,86 9 ″ ″ ″ 332 344 13 FAKYLWEWASVRF 1295 B*4601 75 1,86 139 ″ ″ ″ 335 344 10 YLWEWASVRF 1296 B*1502 90 1,86 167 ″ ″ ″ 335 344 10 YLWEWASVRF ″ B*1525 45 1,86 84 ″ ″ ″ 337 344 8 WEWASVRF 1297 B*3701 80 1,86 149 ″ ″ ″ 337 344 8 WEWASVRF ″ B*4901 80 1,86 149 ″ ″ ″ 337 344 8 WEWASVRF ″ B*5001 50 1,86 93 ″ ″ ″ 337 344 8 WEWASVRF ″ B*1301 45 1,86 84 ″ ″ ″ 337 344 8 WEWASVRF ″ B*4403 5 1,86 9 ″ ″ ″ 337 345 9 WEWASVRFS 1298 B*4403 65 0,50 33 ″ ″ ″ 337 345 9 WEWASVRFS ″ B*5001 60 0,50 30 ″ ″ ″ 337 345 9 WEWASVRFS ″ B*4002 55 0,50 28 ″ ″ ″ 337 345 9 WEWASVRFS ″ B*4901 15 0,50 8 ″ ″ ″ 333 346 14 AKYLWEWASVRFSW 1299 B*4403 35 1,50 52 ″ ″ ″ 334 346 13 KYLWEWASVRFSW 1300 A*2402 95 1,50 142 ″ ″ ″ 334 346 13 KYLWEWASVRFSW ″ A*2301 75 1,50 112 ″ ″ ″ 335 346 12 YLWEWASVRFSW 1301 A*3201 80 1,50 120 ″ ″ ″ 335 346 12 YLWEWASVRFSW ″ B*1302 75 1,50 112 ″ ″ ″ 335 346 12 YLWEWASVRFSW ″ B*5201 45 1,50 67 ″ ″ ″ 337 346 10 WEWASVRFSW 1302 B*1301 100 1,50 150 ″ ″ ″ 337 346 10 WEWASVRFSW ″ B*4402 100 1,50 150 ″ ″ ″ 337 346 10 WEWASVRFSW ″ B*4403 100 1,50 150 ″ ″ ″ 337 346 10 WEWASVRFSW ″ B*1302 90 1,50 135 ″ ″ ″ 337 346 10 WEWASVRFSW ″ B*4002 90 1,50 135 ″ ″ ″ 337 346 10 WEWASVRFSW ″ B*4901 75 1,50 112 ″ ″ ″ 339 346 8 WASVRFSW 1303 B*5801 50 1,50 75 ″ ″ ″ 334 347 14 KYLWEWASVRFSWL 1304 A*2402 90 1,37 123 ″ ″ ″ 334 347 14 KYLWEWASVRFSWL ″ A*2301 40 1,37 55 ″ ″ ″ 335 347 13 YLWEWASVRFSWL 1305 A*0201 100 1,37 137 ″ ″ ″ 335 347 13 YLWEWASVRFSWL ″ A*0206 60 1,37 82 ″ ″ ″ 337 347 11 WEWASVRFSWL 1306 B*4001 95 1,37 130 ″ ″ ″ 337 347 11 WEWASVRFSWL ″ B*3701 90 1,37 123 ″ ″ ″ 337 347 11 WEWASVRFSWL ″ B*5001 90 1,37 123 ″ ″ ″ 337 347 11 WEWASVRFSWL ″ B*4002 85 1,37 117 ″ ″ ″ 337 347 11 WEWASVRFSWL ″ B*4901 85 1,37 117 ″ ″ ″ 337 347 11 WEWASVRFSWL ″ B*1301 80 1,37 110 ″ ″ ″ 337 347 11 WEWASVRFSWL ″ B*4402 55 1,37 75 ″ ″ ″ 337 347 11 WEWASVRFSWL ″ B*1302 10 1,37 14 ″ ″ ″ 339 347 9 WASVRFSWL 1307 B*0801 50 1,37 69 ″ ″ ″ 337 348 12 WEWASVRFSWLS 1308 B*1801 80 0,54 43 ″ ″ ″ 337 348 12 WEWASVRFSWLS ″ B*4002 70 0,54 38 ″ ″ ″ 337 348 12 WEWASVRFSWLS ″ B*4901 45 0,54 24 ″ ″ ″ 337 348 12 WEWASVRFSWLS ″ B*5001 45 0,54 24 ″ ″ ″ 337 348 12 WEWASVRFSWLS ″ B*4403 20 0,54 11 ″ ″ ″ 337 348 12 WEWASVRFSWLS ″ B*3701 5 0,54 3 ″ ″ ″ 341 348 8 SVRFSWLS 1309 A*3001 40 0,54 22 ″ ″ ″ 337 349 13 WEWASVRFSWLSL 1310 B*1801 100 1,61 161 ″ ″ ″ 337 349 13 WEWASVRFSWLSL ″ B*3701 100 1,61 161 ″ ″ ″ 337 349 13 WEWASVRFSWLSL ″ B*4001 100 1,61 161 ″ ″ ″ 337 349 13 WEWASVRFSWLSL ″ B*4002 100 1,61 161 ″ ″ ″ 337 349 13 WEWASVRFSWLSL ″ B*4901 100 1,61 161 ″ ″ ″ 337 349 13 WEWASVRFSWLSL ″ B*5001 100 1,61 161 ″ ″ ″ 337 349 13 WEWASVRFSWLSL ″ B*1301 90 1,61 145 ″ ″ ″ 337 349 13 WEWASVRFSWLSL ″ B*4403 75 1,61 120 ″ ″ ″ 337 349 13 WEWASVRFSWLSL ″ B*4402 70 1,61 112 ″ ″ ″ 339 349 11 WASVRFSWLSL 1311 B*1402 85 1,61 137 ″ ″ ″ 341 349 9 SVRFSWLSL 1312 A*3001 90 1,61 145 ″ ″ ″ 341 349 9 SVRFSWLSL ″ B*0702 80 1,61 129 ″ ″ ″ 342 349 8 VRFSWLSL 1313 B*3901 70 1,61 112 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL 1314 B*3701 95 1,15 109 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*4002 95 1,15 109 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*5001 95 1,15 109 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*1801 90 1,15 104 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*4901 90 1,15 104 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*1301 85 1,15 98 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*4001 80 1,15 92 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*4403 70 1,15 81 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*4801 70 1,15 81 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*4402 60 1,15 69 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*1302 50 1,15 58 ″ ″ ″ 342 350 9 VRFSWLSLL 1315 B*3801 65 1,15 75 ″ ″ ″ 342 350 9 VRFSWLSLL ″ B*2702 20 1,15 23 ″ ″ ″ 339 351 13 WASVRFSWLSLLV 1316 B*5101 30 1,47 44 ″ ″ ″ 341 351 11 SVRFSWLSLLV 1317 A*3001 85 1,47 125 ″ ″ ″ 340 353 14 ASVRFSWLSLLVPF 1318 B*4601 30 0,19 6 ″ ″ ″ 340 353 14 ASVRFSWLSLLVPF ″ B*1525 15 0,19 3 ″ ″ ″ 341 353 13 SVRFSWLSLLVPF 1319 B*1501 80 0,19 15 ″ ″ ″ 341 353 13 SVRFSWLSLLVPF ″ B*1525 60 0,19 11 ″ ″ ″ 341 353 13 SVRFSWLSLLVPF ″ B*1502 25 0,19 5 ″ ″ ″ 341 353 13 SVRFSWLSLLVPF ″ A*3001 20 0,19 4 ″ ″ ″ 342 353 12 VRFSWLSLLVPF 1320 B*2702 65 0,19 12 ″ ″ ″ 342 353 12 VRFSWLSLLVPF ″ B*2705 55 0,19 10 ″ ″ ″ 343 353 11 RFSWLSLLVPF 1321 A*3201 85 0,19 16 ″ ″ ″ 343 353 11 RFSWLSLLVPF ″ A*2402 80 0,19 15 ″ ″ ″ 344 353 10 FSWLSLLVPF 1322 B*4601 100 0,19 19 ″ ″ ″ 344 353 10 FSWLSLLVPF ″ B*1525 55 0,19 10 ″ ″ ″ 346 353 8 WLSLLVPF 1323 B*1502 10 0,19 2 ″ ″ ″ 341 354 14 SVRFSWLSLLVPFV 1324 A*3001 95 1,30 124 ″ ″ ″ 342 354 13 VRFSWLSLLVPFV 1325 B*2705 15 1,30 20 ″ ″ ″ 346 354 9 WLSLLVPFV 1326 A*0201 94 1,30 123 ″ ″ ″ 343 356 14 RFSWLSLLVPFVQW 1327 A*2402 25 1,92 48 ″ ″ ″ 344 356 13 FSWLSLLVPFVQW 1328 B*5801 90 1,92 173 ″ ″ ″ 344 356 13 FSWLSLLVPFVQW ″ B*5701 85 1,92 163 ″ ″ ″ 344 356 13 FSWLSLLVPFVQW ″ B*5802 60 1,92 115 ″ ″ ″ 344 356 13 FSWLSLLVPFVQW ″ B*5201 40 1,92 77 ″ ″ ″ 347 356 10 LSLLVPFVQW 1329 B*5802 80 1,92 154 ″ ″ ″ 344 357 14 FSWLSLLVPFVQWF 1330 B*4601 65 1,38 89 ″ ″ ″ 345 357 13 SWLSLLVPFVQWF 1331 A*2301 45 1,38 62 ″ ″ ″ 345 357 13 SWLSLLVPFVQWF ″ A*2402 35 1,38 48 ″ ″ ″ 347 357 11 LSLLVPFVQWF 1332 B*5802 20 1,38 28 ″ ″ ″ 348 357 10 SLLVPFVQWF 1333 B*1502 50 1,38 69 ″ ″ ″ 349 357 9 LLVPFVQWF 1334 B*1501 45 1,38 62 ″ ″ ″ 349 357 9 LLVPFVQWF ″ B*1525 10 1,38 14 ″ ″ ″ 346 358 13 WLSLLVPFVQWFV 1335 A*0201 80 1,65 132 ″ ″ ″ 346 358 13 WLSLLVPFVQWFV ″ A*0206 25 1,65 41 ″ ″ ″ 349 358 10 LLVP fVQWFV 1336 A*0201 97 1,65 161 ″ ″ ″ 349 358 10 LLVPFVQWFV ″ A*0206 90 1,65 149 ″ ″ ″ 350 358 9 LVPFVQWFV 1337 A*6802 100 1,65 165 ″ ″ ″ 350 358 9 LVPFVQWFV ″ A*0201 43 1,65 71 ″ ″ ″ Cumulative Class I-BCI 13107 score: 328 335 8 SSWAFAKY 1276 A*2501 75 1,90 142 34 328 358 328 335 8 SSWAFAKY ″ A*3002 75 1,90 142 ″ ″ ″ 328 335 8 SSWAFAKY ″ A*2902 55 1,90 104 ″ ″ ″ 328 337 10 SSWAFAKYLW 1280 B*5802 100 1,58 158 ″ ″ ″ 328 337 10 SSWAFAKYLW ″ B*5701 95 1,58 150 ″ ″ ″ 328 337 10 SSWAFAKYLW ″ B*4403 45 1,58 71 ″ ″ ″ 328 337 10 SSWAFAKYLW ″ B*5801 35 1,58 55 ″ ″ ″ 328 337 10 SSWAFAKYLW ″ B*4402 15 1,58 24 ″ ″ ″ 330 337 8 WAFAKYLW 1281 B*5801 85 1,58 134 ″ ″ ″ 330 337 8 WAFAKYLW ″ B*5701 65 1,58 103 ″ ″ ″ 330 337 8 WAFAKYLW ″ B*5802 50 1,58 79 ″ ″ ″ 328 339 12 SSWAFAKYLWEW 1283 B*5701 100 1,83 183 ″ ″ ″ 328 339 12 SSWAFAKYLWEW ″ B*5801 95 1,83 174 ″ ″ ″ 328 339 12 SSWAFAKYLWEW ″ B*5802 65 1,83 119 ″ ″ ″ 328 339 12 SSWAFAKYLWEW ″ A*3201 55 1,83 101 ″ ″ ″ 328 339 12 SSWAFAKYLWEW ″ B*4403 50 1,83 91 ″ ″ ″ 328 339 12 SSWAFAKYLWEW ″ B*4402 10 1,83 18 ″ ″ ″ 330 339 10 WAFAKYLWEW 1284 B*5802 85 1,83 156 ″ ″ ″ 330 339 10 WAFAKYLWEW ″ B*5201 70 1,83 128 ″ ″ ″ 331 339 9 AFAKYLWEW 1285 B*4402 50 1,83 91 ″ ″ ″ 331 339 9 AFAKYLWEW ″ B*4403 40 1,83 73 ″ ″ ″ 332 339 8 FAKYLWEW 1286 B*4601 40 1,83 73 ″ ″ ″ 332 339 8 FAKYLWEW ″ B*5701 30 1,83 55 ″ ″ ″ 330 342 13 WAFAKYLWEWASV 1287 A*6802 85 1,92 164 ″ ″ ″ 330 342 13 WAFAKYLWEWASV ″ B*1402 20 1,92 38 ″ ″ ″ 332 342 11 FAKYLWEWASV 1288 B*4601 50 1,92 96 ″ ″ ″ 330 343 14 WAFAKYLWEWASVR 1289 A*3303 80 1,07 85 ″ ″ ″ 330 343 14 WAFAKYLWEWASVR ″ A*6801 50 1,07 53 ″ ″ ″ 330 343 14 WAFAKYLWEWASVR ″ A*7401 15 1,07 16 ″ ″ ″ 331 343 13 AFAKYLWEWASVR 1290 A*3101 70 1,07 75 ″ ″ ″ 331 343 13 AFAKYLWEWASVR ″ A*3303 35 1,07 37 ″ ″ ″ 332 343 12 FAKYLWEWASVR 1291 A*3303 85 1,07 91 ″ ″ ″ 332 343 12 FAKYLWEWASVR ″ A*6801 60 1,07 64 ″ ″ ″ 332 343 12 FAKYLWEWASVR ″ A*3101 55 1,07 59 ″ ″ ″ 334 343 10 KYLWEWASVR 1292 A*3101 100 1,07 107 ″ ″ ″ 335 343 9 YLWEWASVR 1293 A*7401 85 1,07 91 ″ ″ ″ 335 343 9 YLWEWASVR ″ A*3303 40 1,07 43 ″ ″ ″ 335 343 9 YLWEWASVR ″ A*3101 35 1,07 37 ″ ″ ″ 335 343 9 YLWEWASVR ″ A*0301 20 1,07 21 ″ ″ ″ 331 344 14 AFAKYLWEWASVRF 1294 A*2402 30 1,86 56 ″ ″ ″ 331 344 14 AFAKYLWEWASVRF ″ A*2301 5 1,86 9 ″ ″ ″ 332 344 13 FAKYLWEWASVRF 1295 B*4601 75 1,86 139 ″ ″ ″ 335 344 10 YLWEWASVRF 1296 B*1502 90 1,86 167 ″ ″ ″ 335 344 10 YLWEWASVRF ″ B*1525 45 1,86 84 ″ ″ ″ 337 344 8 WEWASVRF 1297 B*3701 80 1,86 149 ″ ″ ″ 337 344 8 WEWASVRF ″ B*4901 80 1,86 149 ″ ″ ″ 337 344 8 WEWASVRF ″ B*5001 50 1,86 93 ″ ″ ″ 337 344 8 WEWASVRF ″ B*1301 45 1,86 84 ″ ″ ″ 337 344 8 WEWASVRF ″ B*4403 5 1,86 9 ″ ″ ″ 337 345 9 WEWASVRFS 1298 B*4403 65 0,50 33 ″ ″ ″ 337 345 9 WEWASVRFS ″ B*5001 60 0,50 30 ″ ″ ″ 337 345 9 WEWASVRFS ″ B*4002 55 0,50 28 ″ ″ ″ 337 345 9 WEWASVRFS ″ B*4901 15 0,50 8 ″ ″ ″ 333 346 14 AKYLWEWASVRFSW 1299 B*4403 35 1,50 52 ″ ″ ″ 334 346 13 KYLWEWASVRFSW 1300 A*2402 95 1,50 142 ″ ″ ″ 334 346 13 KYLWEWASVRFSW ″ A*2301 75 1,50 112 ″ ″ ″ 335 346 12 YLWEWASVRFSW 1301 A*3201 80 1,50 120 ″ ″ ″ 335 346 12 YLWEWASVRFSW ″ B*1302 75 1,50 112 ″ ″ ″ 335 346 12 YLWEWASVRFSW ″ B*5201 45 1,50 67 ″ ″ ″ 337 346 10 WEWASVRFSW 1302 B*1301 100 1,50 150 ″ ″ ″ 337 346 10 WEWASVRFSW ″ B*4402 100 1,50 150 ″ ″ ″ 337 346 10 WEWASVRFSW ″ B*4403 100 1,50 150 ″ ″ ″ 337 346 10 WEWASVRFSW ″ B*1302 90 1,50 135 ″ ″ ″ 337 346 10 WEWASVRFSW ″ B*4002 90 1,50 135 ″ ″ ″ 337 346 10 WEWASVRFSW ″ B*4901 75 1,50 112 ″ ″ ″ 339 346 8 WASVRFSW 1303 B*5801 50 1,50 75 ″ ″ ″ 334 347 14 KYLWEWASVRFSWL 1304 A*2402 90 1,37 123 ″ ″ ″ 334 347 14 KYLWEWASVRFSWL ″ A*2301 40 1,37 55 ″ ″ ″ 335 347 13 YLWEWASVRFSWL 1305 A*0201 100 1,37 137 ″ ″ ″ 335 347 13 YLWEWASVRFSWL ″ A*0206 60 1,37 82 ″ ″ ″ 337 347 11 WEWASVRFSWL 1306 B*4001 95 1,37 130 ″ ″ ″ 337 347 11 WEWASVRFSWL ″ B*3701 90 1,37 123 ″ ″ ″ 337 347 11 WEWASVRFSWL ″ B*5001 90 1,37 123 ″ ″ ″ 337 347 11 WEWASVRFSWL ″ B*4002 85 1,37 117 ″ ″ ″ 337 347 11 WEWASVRFSWL ″ B*4901 85 1,37 117 ″ ″ ″ 337 347 11 WEWASVRFSWL ″ B*1301 80 1,37 110 ″ ″ ″ 337 347 11 WEWASVRFSWL ″ B*4402 55 1,37 75 ″ ″ ″ 337 347 11 WEWASVRFSWL ″ B*1302 10 1,37 14 ″ ″ ″ 339 347 9 WASVRFSWL 1307 B*0801 50 1,37 69 ″ ″ ″ 337 348 12 WEWASVRFSWLS 1308 B*1801 80 0,54 43 ″ ″ ″ 337 348 12 WEWASVRFSWLS ″ B*4002 70 0,54 38 ″ ″ ″ 337 348 12 WEWASVRFSWLS ″ B*4901 45 0,54 24 ″ ″ ″ 337 348 12 WEWASVRFSWLS ″ B*5001 45 0,54 24 ″ ″ ″ 337 348 12 WEWASVRFSWLS ″ B*4403 20 0,54 11 ″ ″ ″ 337 348 12 WEWASVRFSWLS ″ B*3701 5 0,54 3 ″ ″ ″ 341 348 8 SVRFSWLS 1309 A*3001 40 0,54 22 ″ ″ ″ 337 349 13 WEWASVRFSWLSL 1310 B*1801 100 1,61 161 ″ ″ ″ 337 349 13 WEWASVRFSWLSL ″ B*3701 100 1,61 161 ″ ″ ″ 337 349 13 WEWASVRFSWLSL ″ B*4001 100 1,61 161 ″ ″ ″ 337 349 13 WEWASVRFSWLSL ″ B*4002 100 1,61 161 ″ ″ ″ 337 349 13 WEWASVRFSWLSL ″ B*4901 100 1,61 161 ″ ″ ″ 337 349 13 WEWASVRFSWLSL ″ B*5001 100 1,61 161 ″ ″ ″ 337 349 13 WEWASVRFSWLSL ″ B*1301 90 1,61 145 ″ ″ ″ 337 349 13 WEWASVRFSWLSL ″ B*4403 75 1,61 120 ″ ″ ″ 337 349 13 WEWASVRFSWLSL ″ B*4402 70 1,61 112 ″ ″ ″ 339 349 11 WASVRFSWLSL 1311 B*1402 85 1,61 137 ″ ″ ″ 341 349 9 SVRFSWLSL 1312 A*3001 90 1,61 145 ″ ″ ″ 341 349 9 SVRFSWLSL ″ B*0702 80 1,61 129 ″ ″ ″ 342 349 8 VRFSWLSL 1313 B*3901 70 1,61 112 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL 1314 B*3701 95 1,15 109 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*4002 95 1,15 109 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*5001 95 1,15 109 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*1801 90 1,15 104 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*4901 90 1,15 104 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*1301 85 1,15 98 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*4001 80 1,15 92 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*4403 70 1,15 81 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*4801 70 1,15 81 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*4402 60 1,15 69 ″ ″ ″ 337 350 14 WEWASVRFSWLSLL ″ B*1302 50 1,15 58 ″ ″ ″ 342 350 9 VRFSWLSLL 1315 B*3801 65 1,15 75 ″ ″ ″ 342 350 9 VRFSWLSLL ″ B*2702 20 1,15 23 ″ ″ ″ 339 351 13 WASVRFSWLSLLV 1316 B*5101 30 1,47 44 ″ ″ ″ 341 351 11 SVRFSWLSLLV 1317 A*3001 85 1,47 125 ″ ″ ″ 340 353 14 ASVRFSWLSLLVPF 1318 B*4601 30 0,19 6 ″ ″ ″ 340 353 14 ASVRFSWLSLLVPF ″ B*1525 15 0,19 3 ″ ″ ″ 341 353 13 SVRFSWLSLLVPF 1319 B*1501 80 0,19 15 ″ ″ ″ 341 353 13 SVRFSWLSLLVPF ″ B*1525 60 0,19 11 ″ ″ ″ 341 353 13 SVRFSWLSLLVPF ″ B*1502 25 0,19 5 ″ ″ ″ 341 353 13 SVRFSWLSLLVPF ″ A*3001 20 0,19 4 ″ ″ ″ 342 353 12 VRFSWLSLLVPF 1320 B*2702 65 0,19 12 ″ ″ ″ 342 353 12 VRFSWLSLLVPF ″ B*2705 55 0,19 10 ″ ″ ″ 343 353 11 RFSWLSLLVPF 1321 A*3201 85 0,19 16 ″ ″ ″ 343 353 11 RFSWLSLLVPF ″ A*2402 80 0,19 15 ″ ″ ″ 344 353 10 FSWLSLLVPF 1322 B*4601 100 0,19 19 ″ ″ ″ 344 353 10 FSWLSLLVPF ″ B*1525 55 0,19 10 ″ ″ ″ 346 353 8 WLSLLVPF 1323 B*1502 10 0,19 2 ″ ″ ″ 341 354 14 SVRFSWLSLLVPFV 1324 A*3001 95 1,30 124 ″ ″ ″ 342 354 13 VRFSWLSLLVPFV 1325 B*2705 15 1,30 20 ″ ″ ″ 346 354 9 WLSLLVPFV 1326 A*0201 94 1,30 123 ″ ″ ″ 343 356 14 RFSWLSLLVPFVQW 1327 A*2402 25 1,92 48 ″ ″ ″ 344 356 13 FSWLSLLVPFVQW 1328 B*5801 90 1,92 173 ″ ″ ″ 344 356 13 FSWLSLLVPFVQW ″ B*5701 85 1,92 163 ″ ″ ″ 344 356 13 FSWLSLLVPFVQW ″ B*5802 60 1,92 115 ″ ″ ″ 344 356 13 FSWLSLLVPFVQW ″ B*5201 40 1,92 77 ″ ″ ″ 347 356 10 LSLLVPFVQW 1329 B*5802 80 1,92 154 ″ ″ ″ 344 357 14 FSWLSLLVPFVQWF 1330 B*4601 65 1,38 89 ″ ″ ″ 345 357 13 SWLSLLVPFVQWF 1331 A*2301 45 1,38 62 ″ ″ ″ 345 357 13 SWLSLLVPFVQWF ″ A*2402 35 1,38 48 ″ ″ ″ 347 357 11 LSLLVPFVQWF 1332 B*5802 20 1,38 28 ″ ″ ″ 348 357 10 SLLVPFVQWF 1333 B*1502 50 1,38 69 ″ ″ ″ 349 357 9 LLVPFVQWF 1334 B*1501 45 1,38 62 ″ ″ ″ 349 357 9 LLVPFVQWF ″ B*1525 10 1,38 14 ″ ″ ″ 346 358 13 WLSLLVPFVQWFV 1335 A*0201 80 1,65 132 ″ ″ ″ 346 358 13 WLSLLVPFVQWFV ″ A*0206 25 1,65 41 ″ ″ ″ 349 358 10 LLVPfVQWFV 1336 A*0201 97 1,65 161 ″ ″ ″ 349 358 10 LLVPFVQWFV ″ A*0206 90 1,65 149 ″ ″ ″ 350 358 9 LVPFVQWFV 1337 A*6802 100 1,65 165 ″ ″ ″ 350 358 9 LVPFVQWFV ″ A*0201 43 1,65 71 ″ ″ ″ Cumulative Class I-BCI 12851 score: 366 373 8 LSAIWMMW 1338 B*5801 100 1,78 178 35 365 400 366 373 8 LSAIWMMW ″ B*5701 60 1,78 107 ″ ″ ″ 366 373 8 LSAIWMMW ″ B*5802 45 1,78 80 ″ ″ ″ 365 374 10 WLSAIWMMWY 1339 A*0101 90 1,38 124 ″ ″ ″ 365 374 10 WLSAIWMMWY ″ A*0301 70 1,38 96 ″ ″ ″ 366 374 9 LSAIWMMWY 1340 A*0101 100 1,38 138 ″ ″ ″ 367 374 8 SAIWMMWY 1341 A*2501 90 1,38 124 ″ ″ ″ 367 374 8 SAIWMMWY ″ A*3002 60 1,38 83 ″ ″ ″ 366 375 10 LSAIWMMWYW 1342 B*5802 95 1,46 139 ″ ″ ″ 366 375 10 LSAIWMMWYW ″ B*5801 75 1,46 110 ″ ″ ″ 367 375 9 SAIWMMWYW 1343 B*5801 80 1,46 117 ″ ″ ″ 367 375 9 SAIWMMWYW ″ B*4403 55 1,46 81 ″ ″ ″ 367 375 9 SAIWMMWYW ″ B*5701 55 1,46 81 ″ ″ ″ 367 375 9 SAIWMMWYW ″ B*4402 45 1,46 66 ″ ″ ″ 367 375 9 SAIWMMWYW ″ B*5301 40 1,46 59 ″ ″ ″ 368 375 8 AIWMMWYW 1344 B*5701 25 1,46 37 ″ ″ ″ 370 379 10 WMMWYWGPSL 1345 B*0801 95 1,46 138 ″ ″ ″ 370 379 10 WMMWYWGPSL ″ B*3801 95 1,46 138 ″ ″ ″ 370 379 10 WMMWYWGPSL ″ B*3901 95 1,46 138 ″ ″ ″ 370 379 10 WMMWYWGPSL ″ B*4801 80 1,46 117 ″ ″ ″ 370 379 10 WMMWYWGPSL ″ B*3701 65 1,46 95 ″ ″ ″ 370 379 10 WMMWYWGPSL ″ B*1301 40 1,46 58 ″ ″ ″ 370 379 10 WMMWYWGPSL ″ B*1525 20 1,46 29 ″ ″ ″ 371 379 9 MMWYWGPSL 1346 B*4801 85 1,46 124 ″ ″ ″ 371 379 9 MMWYWGPSL ″ B*1525 75 1,46 109 ″ ″ ″ 371 379 9 MMWYWGPSL ″ A*0201 46 1,46 67 ″ ″ ″ 371 379 9 MMWYWGPSL ″ A*3201 45 1,46 66 ″ ″ ″ 371 379 9 MMWYWGPSL ″ B*1501 40 1,46 58 ″ ″ ″ 371 379 9 MMWYWGPSL ″ B*3901 40 1,46 58 ″ ″ ″ 367 380 14 SAIWMMWYWGPSLY 1347 A*2601 95 1,93 183 ″ ″ ″ 367 380 14 SAIWMMWYWGPSLY ″ A*1101 80 1,93 154 ″ ″ ″ 367 380 14 SAIWMMWYWGPSLY ″ B*3501 75 1,93 145 ″ ″ ″ 368 380 13 AIWMMWYWGPSLY 1348 A*3002 85 1,93 164 ″ ″ ″ 370 380 11 WMMWYWGPSLY 1349 B*1502 100 1,93 193 ″ ″ ″ 370 380 11 WMMWYWGPSLY ″ A*0101 95 1,93 183 ″ ″ ″ 370 380 11 WMMWYWGPSLY ″ B*1501 75 1,93 145 ″ ″ ″ 371 380 10 MMWYWGPSLY 1350 A*0301 100 1,93 193 ″ ″ ″ 371 380 10 MMWYWGPSLY ″ A*3002 90 1,93 174 ″ ″ ″ 371 380 10 MMWYWGPSLY ″ B*1525 90 1,93 174 ″ ″ ″ 371 380 10 MMWYWGPSLY ″ A*7401 80 1,93 154 ″ ″ ″ 371 380 10 MMWYWGPSLY ″ A*2902 65 1,93 125 ″ ″ ″ 372 380 9 MWYWGPSLY 1351 A*2902 100 1,93 193 ″ ″ ″ 369 382 14 IWMMWYWGPSLYSI 1352 A*2402 85 0,77 65 ″ ″ ″ 369 382 14 IWMMWYWGPSLYSI ″ A*2301 60 0,77 46 ″ ″ ″ 370 382 13 WMMWYWGPSLYSI 1353 A*0206 100 0,77 77 ″ ″ ″ 370 382 13 WMMWYWGPSLYSI ″ B*0801 85 0,77 65 ″ ″ ″ 370 382 13 WMMWYWGPSLYSI ″ B*3801 75 0,77 58 ″ ″ ″ 370 382 13 WMMWYWGPSLYSI ″ A*0201 74 0,77 57 ″ ″ ″ 371 382 12 MMWYWGPSLYSI 1354 A*3201 100 0,77 77 ″ ″ ″ 371 382 12 MMWYWGPSLYSI ″ B*5201 100 0,77 77 ″ ″ ″ 371 382 12 MMWYWGPSLYSI ″ B*1302 95 0,77 73 ″ ″ ″ 371 382 12 MMWYWGPSLYSI ″ A*0201 86 0,77 66 ″ ″ ″ 371 382 12 MMWYWGPSLYSI ″ A*7401 75 0,77 58 ″ ″ ″ 371 382 12 MMWYWGPSLYSI ″ B*4801 75 0,77 58 ″ ″ ″ 371 382 12 MMWYWGPSLYSI ″ B*1301 70 0,77 54 ″ ″ ″ 370 383 14 WMMWYWGPSLYSIV 1355 A*0206 70 0,79 55 ″ ″ ″ 370 383 14 WMMWYWGPSLYSIV ″ A*0201 51 0,79 40 ″ ″ ″ 370 383 14 WMMWYWGPSLYSIV ″ B*0801 45 0,79 35 ″ ″ ″ 370 383 14 WMMWYWGPSLYSIV ″ B*3901 10 0,79 8 ″ ″ ″ 370 383 14 WMMWYWGPSLYSIV ″ B*3801 5 0,79 4 ″ ″ ″ 371 383 13 MMWYWGPSLYSIV 1356 A*0201 69 0,79 54 ″ ″ ″ 371 383 13 MMWYWGPSLYSIV ″ B*1302 25 0,79 20 ″ ″ ″ 371 383 13 MMWYWGPSLYSIV ″ B*4801 25 0,79 20 ″ ″ ″ 373 386 14 WYWGPSLYSIVSPF 1357 B*1502 80 0,72 58 ″ ″ ″ 373 386 14 WYWGPSLYSIVSPF ″ A*2301 55 0,72 40 ″ ″ ″ 373 386 14 WYWGPSLYSIVSPF ″ A*2402 20 0,72 14 ″ ″ ″ 373 386 14 WYWGPSLYSIVSPF ″ A*2902 15 0,72 11 ″ ″ ″ 374 386 13 YWGPSLYSIVSPF 1358 A*2301 70 0,72 51 ″ ″ ″ 374 386 13 YWGPSLYSIVSPF ″ A*2402 70 0,72 51 ″ ″ ″ 377 386 10 PSLYSIVSPF 1359 A*3201 35 0,72 25 ″ ″ ″ 378 386 9 SLYSIVSPF 1360 B*1525 95 0,72 69 ″ ″ ″ 378 386 9 SLYSIVSPF ″ A*3201 90 0,72 65 ″ ″ ″ 378 386 9 SLYSIVSPF ″ B*1501 85 0,72 61 ″ ″ ″ 378 386 9 SLYSIVSPF ″ B*4601 20 0,72 14 ″ ″ ″ 378 386 9 SLYSIVSPF ″ A*2601 10 0,72 7 ″ ″ ″ 374 387 14 YWGPSLYSIVSPFI 1361 A*2402 15 1,16 17 ″ ″ ″ 378 387 10 SLYSiVSPFI 1362 A*0201 3 1,16 3 ″ ″ ″ 376 389 14 GPSLYSIVSPFIPL 1363 B*0702 65 0,42 27 ″ ″ ″ 378 389 12 SLYSIVSPFIPL 1364 A*3201 75 0,42 32 ″ ″ ″ 378 389 12 SLYSIVSPFIPL ″ A*0201 34 0,42 14 ″ ″ ″ 378 389 12 SLYSIVSPFIPL ″ B*1502 30 0,42 13 ″ ″ ″ 378 389 12 SLYSIVSPFIPL ″ B*1501 5 0,42 2 ″ ″ ″ 380 389 10 YSIVSPFIPL 1365 B*3901 65 0,42 27 ″ ″ ″ 380 389 10 YSIVSPFIPL ″ A*6802 45 0,42 19 ″ ″ ″ 380 389 10 YSIVSPFIPL ″ B*4001 40 0,42 17 ″ ″ ″ 378 390 13 SLYSIVSPFIPLL 1366 A*0201 17 1,76 30 ″ ″ ″ 379 392 14 LYSIVSPFIPLLPI 1367 A*2402 60 1,07 64 ″ ″ ″ 380 392 13 YSIVSPFIPLLPI 1368 B*4601 45 1,07 48 ″ ″ ″ 380 392 13 YSIVSPFIPLLPI ″ B*5201 30 1,07 32 ″ ″ ″ 381 392 12 SIVSPFIPLLPI 1369 A*6802 25 1,07 27 ″ ″ ″ 382 392 11 IVSPFIPLLPI 1370 A*6802 30 1,07 32 ″ ″ ″ 384 392 9 SPFIPLLPI 1371 B*5501 90 1,07 96 ″ ″ ″ 384 392 9 SPFIPLLPI ″ B*5201 75 1,07 80 ″ ″ ″ 384 392 9 SPFIPLLPI ″ B*5101 70 1,07 75 ″ ″ ″ 384 392 9 SPFIPLLPI ″ B*5601 10 1,07 11 ″ ″ ″ 380 393 14 YSIVSPFIPLLPIF 1372 B*4601 85 0,82 69 ″ ″ ″ 380 393 14 YSIVSPFIPLLPIF ″ B*5801 55 0,82 45 ″ ″ ″ 380 393 14 YSIVSPFIPLLPIF ″ A*2501 45 0,82 37 ″ ″ ″ 380 393 14 YSIVSPFIPLLPIF ″ B*1525 30 0,82 25 ″ ″ ″ 380 393 14 YSIVSPFIPLLPIF ″ B*1501 15 0,82 12 ″ ″ ″ 381 393 13 SIVSPFIPLLPIF 1373 B*1525 40 0,82 33 ″ ″ ″ 381 393 13 SIVSPFIPLLPIF ″ A*2601 5 0,82 4 ″ ″ ″ 384 393 10 SPFIPLLPIF 1374 B*3501 65 0,82 53 ″ ″ ″ 384 393 10 SPFIPLLPIF ″ B*3503 65 0,82 53 ″ ″ ″ 384 393 10 SPFIPLLPIF ″ B*5101 45 0,82 37 ″ ″ ″ 385 393 9 PFIPLLPIF 1375 A*2301 15 0,82 12 ″ ″ ″ 386 393 8 FIPLLPIF 1376 A*2501 20 0,82 16 ″ ″ ″ 384 394 11 SPFIPLLPIFF 1377 B*3503 100 1,11 111 ″ ″ ″ 387 394 8 IPLLPIFF 1378 B*3503 70 1,11 78 ″ ″ ″ 386 395 10 FIPLIPIFFC 1379 A*0201 9 0,98 8 ″ ″ ″ 384 396 13 SPFIPLLPIFFCL 1380 B*3503 75 1,93 145 ″ ″ ″ 387 396 10 IPLLPIFFCL 1381 B*5101 10 1,93 19 ″ ″ ″ 384 397 14 SPFIPLLPIFFCLW 1382 B*3503 60 1,67 100 ″ ″ ″ 384 397 14 SPFIPLLPIFFCLW ″ B*5301 15 1,67 25 ″ ″ ″ 387 397 11 IPLLPIFFCLW 1383 B*5101 55 1,67 92 ″ ″ ″ 387 398 12 IPLLPIFFCLWV 1384 B*5101 100 1,51 151 ″ ″ ″ 389 398 10 LLPIfFCLWV 1385 A*0201 89 1,51 134 ″ ″ ″ 390 398 9 LPIFFCLWV 1386 B*5101 85 1,51 129 ″ ″ ″ 386 399 14 FIPLLPIFFCLWVY 1387 A*2501 50 1,83 92 ″ ″ ″ 386 399 14 FIPLLPIFFCLWVY ″ A*0101 35 1,83 64 ″ ″ ″ 386 399 14 FIPLLPIFFCLWVY ″ A*2601 20 1,83 37 ″ ″ ″ 387 399 13 IPLLPIFFCLWVY 1388 B*3501 60 1,83 110 ″ ″ ″ 388 399 12 PLLPIFFCLWVY 1389 A*2902 25 1,83 46 ″ ″ ″ 388 399 12 PLLPIFFCLWVY ″ A*3002 25 1,83 46 ″ ″ ″ 389 399 11 LLPIFFCLWVY 1390 A*0101 60 1,83 110 ″ ″ ″ 390 399 10 LPIFFCLWVY 1391 B*3501 95 1,83 174 ″ ″ ″ 390 399 10 LPIFFCLWVY ″ B*5101 35 1,83 64 ″ ″ ″ 390 399 10 LPIFFCLWVY ″ B*5301 35 1,83 64 ″ ″ ″ 391 399 9 PIFFCLWVY 1392 A*3002 40 1,83 73 ″ ″ ″ 391 399 9 PIFFCLWVY ″ A*2501 25 1,83 46 ″ ″ ″ 392 399 8 IFFCLWVY 1393 A*3002 35 1,83 64 ″ ″ ″ 387 400 14 IPLLPIFFCLWVYI 1394 B*5101 90 1,45 131 ″ ″ ″ 387 400 14 IPLLPIFFCLWVYI ″ B*5201 20 1,45 29 ″ ″ ″ 390 400 11 LPIFFCLWVYI 1395 B*3503 5 1,45 7 ″ ″ ″ Cumulative Class I-BCI 9736 score: 371 380 10 MMWYWGPSLY 1350 A*0301 100 1,93 193 36 371 400 371 380 10 MMWYWGPSLY ″ A*3002 90 1,93 174 ″ ″ ″ 371 380 10 MMWYWGPSLY ″ B*1525 90 1,93 174 ″ ″ ″ 371 380 10 MMWYWGPSLY ″ A*7401 80 1,93 154 ″ ″ ″ 371 380 10 MMWYWGPSLY ″ A*2902 65 1,93 125 ″ ″ ″ 372 380 9 MWYWGPSLY 1351 A*2902 100 1,93 193 ″ ″ ″ 371 382 12 MMWYWGPSLYSI 1354 A*3201 100 0,77 77 ″ ″ ″ 371 382 12 MMWYWGPSLYSI ″ B*5201 100 0,77 77 ″ ″ ″ 371 382 12 MMWYWGPSLYSI ″ B*1302 95 0,77 73 ″ ″ ″ 371 382 12 MMWYWGPSLYSI ″ A*0201 86 0,77 66 ″ ″ ″ 371 382 12 MMWYWGPSLYSI ″ A*7401 75 0,77 58 ″ ″ ″ 371 382 12 MMWYWGPSLYSI ″ B*4801 75 0,77 58 ″ ″ ″ 371 382 12 MMWYWGPSLYSI ″ B*1301 70 0,77 54 ″ ″ ″ 370 383 14 WMMWYWGPSLYSIV 1355 A*0206 70 0,79 55 ″ ″ ″ 370 383 14 WMMWYWGPSLYSIV ″ A*0201 51 0,79 40 ″ ″ ″ 370 383 14 WMMWYWGPSLYSIV ″ B*0801 45 0,79 35 ″ ″ ″ 370 383 14 WMMWYWGPSLYSIV ″ B*3901 10 0,79 8 ″ ″ ″ 370 383 14 WMMWYWGPSLYSIV ″ B*3801 5 0,79 4 ″ ″ ″ 371 383 13 MMWYWGPSLYSIV 1356 A*0201 69 0,79 54 ″ ″ ″ 371 383 13 MMWYWGPSLYSIV ″ B*1302 25 0,79 20 ″ ″ ″ 371 383 13 MMWYWGPSLYSIV ″ B*4801 25 0,79 20 ″ ″ ″ 373 386 14 WYWGPSLYSIVSPF 1357 B*1502 80 0,72 58 ″ ″ ″ 373 386 14 WYWGPSLYSIVSPF ″ A*2301 55 0,72 40 ″ ″ ″ 373 386 14 WYWGPSLYSIVSPF ″ A*2402 20 0,72 14 ″ ″ ″ 373 386 14 WYWGPSLYSIVSPF ″ A*2902 15 0,72 11 ″ ″ ″ 374 386 13 YWGPSLYSIVSPF 1358 A*2301 70 0,72 51 ″ ″ ″ 374 386 13 YWGPSLYSIVSPF ″ A*2402 70 0,72 51 ″ ″ ″ 377 386 10 PSLYSIVSPF 1359 A*3201 35 0,72 25 ″ ″ ″ 378 386 9 SLYSIVSPF 1360 B*1525 95 0,72 69 ″ ″ ″ 378 386 9 SLYSIVSPF ″ A*3201 90 0,72 65 ″ ″ ″ 378 386 9 SLYSIVSPF ″ B*1501 85 0,72 61 ″ ″ ″ 378 386 9 SLYSIVSPF ″ B*4601 20 0,72 14 ″ ″ ″ 378 386 9 SLYSIVSPF ″ A*2601 10 0,72 7 ″ ″ ″ 374 387 14 YWGPSLYSIVSPFI 1361 A*2402 15 1,16 17 ″ ″ ″ 378 387 10 SLYSiVSPFI 1362 A*0201 3 1,16 3 ″ ″ ″ 376 389 14 GPSLYSIVSPFIPL 1363 B*0702 65 0,42 27 ″ ″ ″ 378 389 12 SLYSIVSPFIPL 1364 A*3201 75 0,42 32 ″ ″ ″ 378 389 12 SLYSIVSPFIPL ″ A*0201 34 0,42 14 ″ ″ ″ 378 389 12 SLYSIVSPFIPL ″ B*1502 30 0,42 13 ″ ″ ″ 378 389 12 SLYSIVSPFIPL ″ B*1501 5 0,42 2 ″ ″ ″ 380 389 10 YSIVSPFIPL 1365 B*3901 65 0,42 27 ″ ″ ″ 380 389 10 YSIVSPFIPL ″ A*6802 45 0,42 19 ″ ″ ″ 380 389 10 YSIVSPFIPL ″ B*4001 40 0,42 17 ″ ″ ″ 378 390 13 SLYSIVSPFIPLL 1366 A*0201 17 1,76 30 ″ ″ ″ 379 392 14 LYSIVSPFIPLLPI 1367 A*2402 60 1,07 64 ″ ″ ″ 380 392 13 YSIVSPFIPLLPI 1368 B*4601 45 1,07 48 ″ ″ ″ 380 392 13 YSIVSPFIPLLPI ″ B*5201 30 1,07 32 ″ ″ ″ 381 392 12 SIVSPFIPLLPI 1369 A*6802 25 1,07 27 ″ ″ ″ 382 392 11 IVSPFIPLLPI 1370 A*6802 30 1,07 32 ″ ″ ″ 384 392 9 SPFIPLLPI 1371 B*5501 90 1,07 96 ″ ″ ″ 384 392 9 SPFIPLLPI ″ B*5201 75 1,07 80 ″ ″ ″ 384 392 9 SPFIPLLPI ″ B*5101 70 1,07 75 ″ ″ ″ 384 392 9 SPFIPLLPI ″ B*5601 10 1,07 11 ″ ″ ″ 380 393 14 YSIVSPFIPLLPIF 1372 B*4601 85 0,82 69 ″ ″ ″ 380 393 14 YSIVSPFIPLLPIF ″ B*5801 55 0,82 45 ″ ″ ″ 380 393 14 YSIVSPFIPLLPIF ″ A*2501 45 0,82 37 ″ ″ ″ 380 393 14 YSIVSPFIPLLPIF ″ B*1525 30 0,82 25 ″ ″ ″ 380 393 14 YSIVSPFIPLLPIF ″ B*1501 15 0,82 12 ″ ″ ″ 381 393 13 SIVSPFIPLLPIF 1373 B*1525 40 0,82 33 ″ ″ ″ 381 393 13 SIVSPFIPLLPIF ″ A*2601 5 0,82 4 ″ ″ ″ 384 393 10 SPFIPLLPIF 1374 B*3501 65 0,82 53 ″ ″ ″ 384 393 10 SPFIPLLPIF ″ B*3503 65 0,82 53 ″ ″ ″ 384 393 10 SPFIPLLPIF ″ B*5101 45 0,82 37 ″ ″ ″ 385 393 9 PFIPLLPIF 1375 A*2301 15 0,82 12 ″ ″ ″ 386 393 8 FIPLLPIF 1376 A*2501 20 0,82 16 ″ ″ ″ 384 394 11 SPFIPLLPIFF 1377 B*3503 100 1,11 111 ″ ″ ″ 387 394 8 IPLLPIFF 1378 B*3503 70 1,11 78 ″ ″ ″ 386 395 10 FIPLIPIFFC 1379 A*0201 9 0,98 8 ″ ″ ″ 384 396 13 SPFIPLLPIFFCL 1380 B*3503 75 1,93 145 ″ ″ ″ 387 396 10 IPLLPIFFCL 1381 B*5101 10 1,93 19 ″ ″ ″ 384 397 14 SPFIPLLPIFFCLW 1382 B*3503 60 1,67 100 ″ ″ ″ 384 397 14 SPFIPLLPIFFCLW , B*5301 15 1,67 25 ″ ″ ″ 387 397 11 IPLLPIFFCLW 1383 B*5101 55 1,67 92 ″ ″ ″ 387 398 12 IPLLPIFFCLWV 1384 B*5101 100 1,51 151 ″ ″ ″ 389 398 10 LLPIfFCLWV 1385 A*0201 89 1,51 134 ″ ″ ″ 390 398 9 LPIFFCLWV 1386 B*5101 85 1,51 129 ″ ″ ″ 386 399 14 FIPLLPIFFCLWVY 1387 A*2501 50 1,83 92 ″ ″ ″ 386 399 14 FIPLLPIFFCLWVY ″ A*0101 35 1,83 64 ″ ″ ″ 386 399 14 FIPLLPIFFCLWVY ″ A*2601 20 1,83 37 ″ ″ ″ 387 399 13 IPLLPIFFCLWVY 1388 B*3501 60 1,83 110 ″ ″ ″ 388 399 12 PLLPIFFCLWVY 1389 A*2902 25 1,83 46 ″ ″ ″ 388 399 12 PLLPIFFCLWVY ″ A*3002 25 1,83 46 ″ ″ ″ 389 399 11 LLPIFFCLWVY 1390 A*0101 60 1,83 110 ″ ″ ″ 390 399 10 LPIFFCLWVY 1391 B*3501 95 1,83 174 ″ ″ ″ 390 399 10 LPIFFCLWVY ″ B*5101 35 1,83 64 ″ ″ ″ 390 399 10 LPIFFCLWVY ″ B*5301 35 1,83 64 ″ ″ ″ 391 399 9 PIFFCLWVY 1392 A*3002 40 1,83 73 ″ ″ ″ 391 399 9 PIFFCLWVY ″ A*2501 25 1,83 46 ″ ″ ″ 392 399 8 IFFCLWVY 1393 A*3002 35 1,83 64 ″ ″ ″ 387 400 14 IPLLPIFFCLWVYI 1394 B*5101 90 1,45 131 ″ ″ ″ 387 400 14 IPLLPIFFCLWVYI ″ B*5201 20 1,45 29 ″ ″ ″ 390 400 11 LPIFFCLWVYI 1395 B*3503 5 1,45 7 ″ ″ ″ Cumulative Class I-BCI 5389 score: 370 379 10 WMMWYWGPSL 1345 B*0801 95 1,46 138 ″ ″ ″ 370 379 10 WMMWYWGPSL ″ B*3801 95 1,46 138 ″ ″ ″ 370 379 10 WMMWYWGPSL ″ B*3901 95 1,46 138 ″ ″ ″ 370 379 10 WMMWYWGPSL ″ B*4801 80 1,46 117 ″ ″ ″ 370 379 10 WMMWYWGPSL ″ B*3701 65 1,46 95 ″ ″ ″ 370 379 10 WMMWYWGPSL ″ B*1301 40 1,46 58 ″ ″ ″ 370 379 10 WMMWYWGPSL ″ B*1525 20 1,46 29 ″ ″ ″ 370 380 11 WMMWYWGPSLY 1349 B*1502 100 1,93 193 ″ ″ ″ 370 380 11 WMMWYWGPSLY ″ A*0101 95 1,93 183 ″ ″ ″ 370 380 11 WMMWYWGPSLY ″ B*1501 75 1,93 145 ″ ″ ″ 371 380 10 MMWYWGPSLY 1350 A*0301 100 1,93 193 ″ ″ ″ 371 380 10 MMWYWGPSLY ″ A*3002 90 1,93 174 ″ ″ ″ 371 380 10 MMWYWGPSLY ″ B*1525 90 1,93 174 ″ ″ ″ 371 380 10 MMWYWGPSLY ″ A*7401 80 1,93 154 ″ ″ ″ 371 380 10 MMWYWGPSLY ″ A*2902 65 1,93 125 ″ ″ ″ 372 380 9 MWYWGPSLY 1351 A*2902 100 1,93 193 ″ ″ ″ 370 382 13 WMMWYWGPSLYSI 1353 A*0206 100 0,77 77 ″ ″ ″ 370 382 13 WMMWYWGPSLYSI ″ B*0801 85 0,77 65 ″ ″ ″ 370 382 13 WMMWYWGPSLYSI ″ B*3801 75 0,77 58 ″ ″ ″ 370 382 13 WMMWYWGPSLYSI ″ A*0201 74 0,77 57 ″ ″ ″ 371 382 12 MMWYWGPSLYSI 1354 A*3201 100 0,77 77 ″ ″ ″ 371 382 12 MMWYWGPSLYSI ″ B*5201 100 0,77 77 ″ ″ ″ 371 382 12 MMWYWGPSLYSI ″ B*1302 95 0,77 73 ″ ″ ″ 371 382 12 MMWYWGPSLYSI ″ A*0201 86 0,77 66 ″ ″ ″ 371 382 12 MMWYWGPSLYSI ″ A*7401 75 0,77 58 ″ ″ ″ 371 382 12 MMWYWGPSLYSI ″ B*4801 75 0,77 58 ″ ″ ″ 371 382 12 MMWYWGPSLYSI ″ B*1301 70 0,77 54 ″ ″ ″ 370 383 14 WMMWYWGPSLYSIV 1355 A*0206 70 0,79 55 ″ ″ ″ 370 383 14 WMMWYWGPSLYSIV ″ A*0201 51 0,79 40 ″ ″ ″ 370 383 14 WMMWYWGPSLYSIV ″ B*0801 45 0,79 35 ″ ″ ″ 370 383 14 WMMWYWGPSLYSIV ″ B*3901 10 0,79 8 ″ ″ ″ 370 383 14 WMMWYWGPSLYSIV ″ B*3801 5 0,79 4 ″ ″ ″ 371 383 13 MMWYWGPSLYSIV 1356 A*0201 69 0,79 54 ″ ″ ″ 371 383 13 MMWYWGPSLYSIV ″ B*1302 25 0,79 20 ″ ″ ″ 371 383 13 MMWYWGPSLYSIV ″ B*4801 25 0,79 20 ″ ″ ″ 373 386 14 WYWGPSLYSIVSPF 1357 B*1502 80 0,72 58 ″ ″ ″ 373 386 14 WYWGPSLYSIVSPF ″ A*2301 55 0,72 40 ″ ″ ″ 373 386 14 WYWGPSLYSIVSPF ″ A*2402 20 0,72 14 ″ ″ ″ 373 386 14 WYWGPSLYSIVSPF ″ A*2902 15 0,72 11 ″ ″ ″ 374 386 13 YWGPSLYSIVSPF 1358 A*2301 70 0,72 51 ″ ″ ″ 374 386 13 YWGPSLYSIVSPF ″ A*2402 70 0,72 51 ″ ″ ″ 377 386 10 PSLYSIVSPF 1359 A*3201 35 0,72 25 ″ ″ ″ 378 386 9 SLYSIVSPF 1360 B*1525 95 0,72 69 ″ ″ ″ 378 386 9 SLYSIVSPF ″ A*3201 90 0,72 65 ″ ″ ″ 378 386 9 SLYSIVSPF ″ B*1501 85 0,72 61 ″ ″ ″ 378 386 9 SLYSIVSPF ″ B*4601 20 0,72 14 ″ ″ ″ 378 386 9 SLYSIVSPF ″ A*2601 10 0,72 7 ″ ″ ″ 374 387 14 YWGPSLYSIVSPFI 1361 A*2402 15 1,16 17 ″ ″ ″ 378 387 10 SLYSiVSPFI 1362 A*0201 3 1,16 3 ″ ″ ″ 376 389 14 GPSLYSIVSPFIPL 1363 B*0702 65 0,42 27 ″ ″ ″ 378 389 12 SLYSIVSPFIPL 1364 A*3201 75 0,42 32 ″ ″ ″ 378 389 12 SLYSIVSPFIPL ″ A*0201 34 0,42 14 ″ ″ ″ 378 389 12 SLYSIVSPFIPL ″ B*1502 30 0,42 13 ″ ″ ″ 378 389 12 SLYSIVSPFIPL ″ B*1501 5 0,42 2 ″ ″ ″ 380 389 10 YSIVSPFIPL 1365 B*3901 65 0,42 27 ″ ″ ″ 380 389 10 YSIVSPFIPL ″ A*6802 45 0,42 19 ″ ″ ″ 380 389 10 YSIVSPFIPL ″ B*4001 40 0,42 17 ″ ″ ″ 378 390 13 SLYSIVSPFIPLL 1366 A*0201 17 1,76 30 ″ ″ ″ 379 392 14 LYSIVSPFIPLLPI 1367 A*2402 60 1,07 64 ″ ″ ″ 380 392 13 YSIVSPFIPLLPI 1368 B*4601 45 1,07 48 ″ ″ ″ 380 392 13 YSIVSPFIPLLPI ″ B*5201 30 1,07 32 ″ ″ ″ 381 392 12 SIVSPFIPLLPI 1369 A*6802 25 1,07 27 ″ ″ ″ 382 392 11 IVSPFIPLLPI 1370 A*6802 30 1,07 32 ″ ″ ″ 384 392 9 SPFIPLLPI 1371 B*5501 90 1,07 96 ″ ″ ″ 384 392 9 SPFIPLLPI ″ B*5201 75 1,07 80 ″ ″ ″ 384 392 9 SPFIPLLPI ″ B*5101 70 1,07 75 ″ ″ ″ 384 392 9 SPFIPLLPI ″ B*5601 10 1,07 11 ″ ″ ″ 380 393 14 YSIVSPFIPLLPIF 1372 B*4601 85 0,82 69 ″ ″ ″ 380 393 14 YSIVSPFIPLLPIF ″ B*5801 55 0,82 45 ″ ″ ″ 380 393 14 YSIVSPFIPLLPIF ″ A*2501 45 0,82 37 ″ ″ ″ 380 393 14 YSIVSPFIPLLPIF ″ B*1525 30 0,82 25 ″ ″ ″ 380 393 14 YSIVSPFIPLLPIF ″ B*1501 15 0,82 12 ″ ″ ″ 381 393 13 SIVSPFIPLLPIF 1373 B*1525 40 0,82 33 ″ ″ ″ 381 393 13 SIVSPFIPLLPIF ″ A*2601 5 0,82 4 ″ ″ ″ 384 393 10 SPFIPLLPIF 1374 B*3501 65 0,82 53 ″ ″ ″ 384 393 10 SPFIPLLPIF ″ B*3503 65 0,82 53 ″ ″ ″ 384 393 10 SPFIPLLPIF ″ B*5101 45 0,82 37 ″ ″ ″ 385 393 9 PFIPLLPIF 1375 A*2301 15 0,82 12 ″ ″ ″ 386 393 8 FIPLLPIF 1376 A*2501 20 0,82 16 ″ ″ ″ 384 394 11 SPFIPLLPIFF 1377 B*3503 100 1,11 111 ″ ″ ″ 387 394 8 IPLLPIFF 1378 B*3503 70 1,11 78 ″ ″ ″ 386 395 10 FIPLIPIFFC 1379 A*0201 9 0,98 8 ″ ″ ″ 384 396 13 SPFIPLLPIFFCL 1380 B*3503 75 1,93 145 ″ ″ ″ 387 396 10 IPLLPIFFCL 1381 B*5101 10 1,93 19 ″ ″ ″ 384 397 14 SPFIPLLPIFFCLW 1382 B*3503 60 1,67 100 ″ ″ ″ 384 397 14 SPFIPLLPIFFCLW ″ B*5301 15 1,67 25 ″ ″ ″ 387 397 11 IPLLPIFFCLW 1383 B*5101 55 1,67 92 ″ ″ ″ 387 398 12 IPLLPIFFCLWV 1384 B*5101 100 1,51 151 ″ ″ ″ 389 398 10 LLPIfFCLWV 1385 A*0201 89 1,51 134 ″ ″ ″ 390 398 9 LPIFFCLWV 1386 B*5101 85 1,51 129 ″ ″ ″ 386 399 14 FIPLLPIFFCLWVY 1387 A*2501 50 1,83 92 ″ ″ ″ 386 399 14 FIPLLPIFFCLWVY ″ A*0101 35 1,83 64 ″ ″ ″ 386 399 14 FIPLLPIFFCLWVY ″ A*2601 20 1,83 37 ″ ″ ″ 387 399 13 IPLLPIFFCLWVY 1388 B*3501 60 1,83 110 ″ ″ ″ 388 399 12 PLLPIFFCLWVY 1389 A*2902 25 1,83 46 ″ ″ ″ 388 399 12 PLLPIFFCLWVY ″ A*3002 25 1,83 46 ″ ″ ″ 389 399 11 LLPIFFCLWVY 1390 A*0101 60 1,83 110 ″ ″ ″ 390 399 10 LPIFFCLWVY 1391 B*3501 95 1,83 174 ″ ″ ″ 390 399 10 LPIFFCLWVY ″ B*5101 35 1,83 64 ″ ″ ″ 390 399 10 LPIFFCLWVY ″ B*5301 35 1,83 64 ″ ″ ″ 391 399 9 PIFFCLWVY 1392 A*3002 40 1,83 73 ″ ″ ″ 391 399 9 PIFFCLWVY ″ A*2501 25 1,83 46 ″ ″ ″ 392 399 8 IFFCLWVY 1393 A*3002 35 1,83 64 ″ ″ ″ 387 400 14 IPLLPIFFCLWVYI 1394 B*5101 90 1,45 131 ″ ″ ″ 387 400 14 IPLLPIFFCLWVYI ″ B*5201 20 1,45 29 ″ ″ ″ 390 400 11 LPIFFCLWVYI 1395 B*3503 5 1,45 7 ″ ″ ″ Cumulative Class I-BCI 6880 score: ″Start″ and ″End″ are relative to the amino acid sequence of HBV large surface protein as depicted in SEQ ID NO: 1141 ^(A)Peptide amino acid sequence. Each HLA class I binding peptide of HBV large surface protein is listed separately for each HLA class I molecule to which it is predicted to bind, and can be listed multiple times for that reason. ^(B)Class I-B score. See Material and Methods (Examples section). ^(C)C-score. See Material and Methods (Examples section). ^(D)Class I-BCI score. See Material and Methods (Examples section). ^(E)Cumulative Class I-BCI score. See Material and Methods (Examples section).

TABLE 7b Predicted HLA class II-restricted CD4⁺ T cell epitopes contained in SLP sequences from HBV large surface protein. HLA class II binding peptides in SLP derived from HBV Surface antigen HLA- Peptide of invention (SLP) SEQ ID DRB1 Class II- SLP SLP Start End Sequence^(A) NO: molecule B score^(B) SLP# Start End 181 195 GFLGPLLVLQAGFFL 1396 *1501 85 30 175 210 181 195 GFLGPLLVLQAGFFL ″ *0101 60 ″ ″ ″ 181 195 GFLGPLLVLQAGFFL ″ *1301 53 ″ ″ ″ 181 195 GFLGPLLVLQAGFFL ″ *0102 8 ″ ″ ″ 182 196 FLGPLLVLQAGFFLL 1397 *0101 93 ″ ″ ″ 182 196 FLGPLLVLQAGFFLL ″ *1501 83 ″ ″ ″ 182 196 FLGPLLVLQAGFFLL ″ *1301 50 ″ ″ ″ 182 196 FLGPLLVLQAGFFLL ″ *0102 35 ″ ″ ″ 182 196 FLGPLLVLQAGFFLL ″ *0104 28 ″ ″ ″ 182 196 FLGPLLVLQAGFFLL ″ *0106 20 ″ ″ ″ 183 197 LGPLLVLQAGFFLLT 1398 *0101 90 ″ ″ ″ 183 197 LGPLLVLQAGFFLLT ″ *1501 80 ″ ″ ″ 183 197 LGPLLVLQAGFFLLT ″ *1301 48 ″ ″ ″ 183 197 LGPLLVLQAGFFLLT ″ *0104 30 ″ ″ ″ 183 197 LGPLLVLQAGFFLLT ″ *0102 13 ″ ″ ″ 183 197 LGPLLVLQAGFFLLT ″ *0106 8 ″ ″ ″ 184 198 GPLLVLQAGFFLLTR 1399 *1501 78 ″ ″ ″ 184 198 GPLLVLQAGFFLLTR ″ *0101 58 ″ ″ ″ 184 198 GPLLVLQAGFFLLTR ″ *1301 45 ″ ″ ″ 184 198 GPLLVLQAGFFLLTR ″ *0104 33 ″ ″ ″ 184 198 GPLLVLQAGFFLLTR ″ *0102 10 ″ ″ ″ 184 198 GPLLVLQAGFFLLTR ″ *0106 3 ″ ″ ″ 185 199 PLLVLQAGFFLLTRI 1400 *1501 75 ″ ″ ″ 185 199 PLLVLQAGFFLLTRI ″ *1301 43 ″ ″ ″ 185 199 PLLVLQAGFFLLTRI ″ *0101 13 ″ ″ ″ 186 200 LLVLQAGFFLLTRIL 1401 *1301 40 ″ ″ ″ 186 200 LLVLQAGFFLLTRIL ″ *1501 25 ″ ″ ″ 187 201 LVLQAGFFLLTRILT 1402 *1101 83 ″ ″ ″ 187 201 LVLQAGFFLLTRILT ″ *0101 40 ″ ″ ″ 187 201 LVLQAGFFLLTRILT ″ *0701 40 ″ ″ ″ 187 201 LVLQAGFFLLTRILT ″ *1301 38 ″ ″ ″ 187 201 LVLQAGFFLLTRILT ″ *1501 15 ″ ″ ″ 187 201 LVLQAGFFLLTRILT ″ *0301 10 ″ ″ ″ 188 202 VLQAGFFLLTRILTI 1403 *0401 93 ″ ″ ″ 188 202 VLQAGFFLLTRILTI ″ *0701 80 ″ ″ ″ 188 202 VLQAGFFLLTRILTI ″ *1101 80 ″ ″ ″ 188 202 VLQAGFFLLTRILTI ″ *0101 70 ″ ″ ″ 188 202 VLQAGFFLLTRILTI ″ *0104 20 ″ ″ ″ 188 202 VLQAGFFLLTRILTI ″ *0102 15 ″ ″ ″ 189 203 LQAGFFLLTRILTIP 1404 *0401 90 ″ ″ ″ 189 203 LQAGFFLLTRILTIP ″ *0701 78 ″ ″ ″ 189 203 LQAGFFLLTRILTIP ″ *1101 78 ″ ″ ″ 189 203 LQAGFFLLTRILTIP ″ *0101 50 ″ ″ ″ 189 203 LQAGFFLLTRILTIP ″ *0104 35 ″ ″ ″ 189 203 LQAGFFLLTRILTIP ″ *0102 33 ″ ″ ″ 190 204 QAGFFLLTRILTIPQ 1405 *0401 100 ″ ″ ″ 190 204 QAGFFLLTRILTIPQ ″ *0701 75 ″ ″ ″ 190 204 QAGFFLLTRILTIPQ , *1101 75 ″ ″ ″ 190 204 QAGFFLLTRILTIPQ ″ *0101 68 ″ ″ ″ 190 204 QAGFFLLTRILTIPQ ″ *0102 63 ″ ″ ″ 190 204 QAGFFLLTRILTIPQ ″ *0104 58 ″ ″ ″ 190 204 QAGFFLLTRILTIPQ ″ *1501 20 ″ ″ ″ 190 204 QAGFFLLTRILTIPQ ″ *0105 8 ″ ″ ″ 190 204 QAGFFLLTRILTIPQ ″ *0107 8 ″ ″ ″ 191 205 AGFFLLTRILTIPQS 1406 *0401 98 ″ ″ ″ 191 205 AGFFLLTRILTIPQS ″ *0701 73 ″ ″ ″ 191 205 AGFFLLTRILTIPQS ″ *1101 73 ″ ″ ″ 191 205 AGFFLLTRILTIPQS ″ *0102 70 ″ ″ ″ 191 205 AGFFLLTRILTIPQS ″ *0104 65 ″ ″ ″ 191 205 AGFFLLTRILTIPQS ″ *0101 55 ″ ″ ″ 191 205 AGFFLLTRILTIPQS ″ *0106 23 ″ ″ ″ 191 205 AGFFLLTRILTIPQS ″ *0105 10 ″ ″ ″ 191 205 AGFFLLTRILTIPQS ″ *0107 10 ″ ″ ″ 192 206 GFFLLTRILTIPQSL 1407 *0401 95 ″ ″ ″ 192 206 GFFLLTRILTIPQSL ″ *1301 85 ″ ″ ″ 192 206 GFFLLTRILTIPQSL ″ *0102 83 ″ ″ ″ 192 206 GFFLLTRILTIPQSL ″ *0104 80 ″ ″ ″ 192 206 GFFLLTRILTIPQSL ″ *0701 70 ″ ″ ″ 192 206 GFFLLTRILTIPQSL ″ *1101 70 ″ ″ ″ 192 206 GFFLLTRILTIPQSL ″ *0106 50 ″ ″ ″ 192 206 GFFLLTRILTIPQSL ″ *0105 28 ″ ″ ″ 192 206 GFFLLTRILTIPQSL ″ *0107 28 ″ ″ ″ 192 206 GFFLLTRILTIPQSL ″ *0101 18 ″ ″ ″ 192 206 GFFLLTRILTIPQSL ″ *1501 10 ″ ″ ″ 193 207 FFLLTRILTIPQSLD 1408 *0401 88 ″ ″ ″ 193 207 FFLLTRILTIPQSLD ″ *0102 75 ″ ″ ″ 193 207 FFLLTRILTIPQSLD ″ *1301 75 ″ ″ ″ 193 207 FFLLTRILTIPQSLD ″ *0701 68 ″ ″ ″ 193 207 FFLLTRILTIPQSLD ″ *1101 68 ″ ″ ″ 193 207 FFLLTRILTIPQSLD ″ *0104 63 ″ ″ ″ 193 207 FFLLTRILTIPQSLD ″ *0106 48 ″ ″ ″ 193 207 FFLLTRILTIPQSLD ″ *0101 18 ″ ″ ″ 193 207 FFLLTRILTIPQSLD ″ *0105 18 ″ ″ ″ 193 207 FFLLTRILTIPQSLD ″ *0107 18 ″ ″ ″ 194 208 FLLTRILTIPQSLDS 1409 *0401 85 ″ ″ ″ 194 208 FLLTRILTIPQSLDS ″ *1301 65 ″ ″ ″ 194 208 FLLTRILTIPQSLDS ″ *0102 58 ″ ″ ″ 194 208 FLLTRILTIPQSLDS ″ *1101 53 ″ ″ ″ 194 208 FLLTRILTIPQSLDS ″ *0106 43 ″ ″ ″ 194 208 FLLTRILTIPQSLDS ″ *0104 40 ″ ″ ″ 194 208 FLLTRILTIPQSLDS ″ *0701 3 ″ ″ ″ 195 209 LLTRILTIPQSLDSW ″ *1301 70 ″ ″ ″ 195 209 LLTRILTIPQSLDSW ″ *0102 45 ″ ″ ″ 195 209 LLTRILTIPQSLDSW ″ *0106 35 ″ ″ ″ 195 209 LLTRILTIPQSLDSW 1410 *0401 15 ″ ″ ″ 196 210 LTRILTIPQSLDSWW 1411 *1301 45 ″ ″ ″ 4798 Cumulative Class II-B score: 240 254 PPICPGYRWMCLRRF 1412 *1301 83 31 239 274 240 254 PPICPGYRWMCLRRF ″ *1101 70 ″ ″ ″ 241 255 PICPGYRWMCLRRFI 1413 *1301 80 ″ ″ ″ 241 255 PICPGYRWMCLRRFI ″ *1101 80 ″ ″ ″ 241 255 PICPGYRWMCLRRFI ″ *1501 60 ″ ″ ″ 241 255 PICPGYRWMCLRRFI ″ *0701 35 ″ ″ ″ 242 256 ICPGYRWMCLRRFII 1414 *1301 78 ″ ″ ″ 242 256 ICPGYRWMCLRRFII ″ *1501 95 ″ ″ ″ 242 256 ICPGYRWMCLRRFII ″ *1101 90 ″ ″ ″ 242 256 ICPGYRWMCLRRFII ″ *0701 85 ″ ″ ″ 242 256 ICPGYRWMCLRRFII ″ *0104 70 ″ ″ ″ 242 256 ICPGYRWMCLRRFII ″ *0102 68 ″ ″ ″ 242 256 ICPGYRWMCLRRFII ″ *0101 50 ″ ″ ″ 242 256 ICPGYRWMCLRRFII ″ *0105 50 ″ ″ ″ 242 256 ICPGYRWMCLRRFII ″ *0107 50 ″ ″ ″ 242 256 ICPGYRWMCLRRFII ″ *0301 35 ″ ″ ″ 243 257 CPGYRWMCLRRFIIF 1415 *1301 75 ″ ″ ″ 243 257 CPGYRWMCLRRFIIF ″ *1101 5 ″ ″ ″ 243 257 CPGYRWMCLRRFIIF ″ *1501 100 ″ ″ ″ 243 257 CPGYRWMCLRRFIIF ″ *0701 95 ″ ″ ″ 243 257 CPGYRWMCLRRFIIF ″ *0104 85 ″ ″ ″ 243 257 CPGYRWMCLRRFIIF ″ *0102 80 ″ ″ ″ 243 257 CPGYRWMCLRRFIIF ″ *0101 58 ″ ″ ″ 243 257 CPGYRWMCLRRFIIF ″ *0105 58 ″ ″ ″ 243 257 CPGYRWMCLRRFIIF ″ *0107 58 ″ ″ ″ 243 257 CPGYRWMCLRRFIIF ″ *0301 40 ″ ″ ″ 244 258 PGYRWMCLRRFIIFL 1416 *1301 73 ″ ″ ″ 244 258 PGYRWMCLRRFIIFL ″ *1101 95 ″ ″ ″ 244 258 PGYRWMCLRRFIIFL ″ *1501 90 ″ ″ ″ 244 258 PGYRWMCLRRFIIFL ″ *0701 80 ″ ″ ″ 244 258 PGYRWMCLRRFIIFL ″ *0104 75 ″ ″ ″ 244 258 PGYRWMCLRRFIIFL ″ *0102 73 ″ ″ ″ 244 258 PGYRWMCLRRFIIFL ″ *0101 45 ″ ″ ″ 244 258 PGYRWMCLRRFIIFL ″ *0105 45 ″ ″ ″ 244 258 PGYRWMCLRRFIIFL ″ *0107 45 ″ ″ ″ 244 258 PGYRWMCLRRFIIFL ″ *0301 15 ″ ″ ″ 245 259 GYRWMCLRRFIIFLF 1417 *1301 100 ″ ″ ″ 245 259 GYRWMCLRRFIIFLF ″ *0701 48 ″ ″ ″ 245 259 GYRWMCLRRFIIFLF ″ *1501 20 ″ ″ ″ 245 259 GYRWMCLRRFIIFLF ″ *1101 85 ″ ″ ″ 245 259 GYRWMCLRRFIIFLF ″ *0102 60 ″ ″ ″ 245 259 GYRWMCLRRFIIFLF ″ *0104 60 ″ ″ ″ 245 259 GYRWMCLRRFIIFLF ″ *0101 30 ″ ″ ″ 245 259 GYRWMCLRRFIIFLF ″ *0105 30 ″ ″ ″ 245 259 GYRWMCLRRFIIFLF ″ *0107 30 ″ ″ ″ 246 260 YRWMCLRRFIIFLFI ″ *1301 98 ″ ″ ″ 246 260 YRWMCLRRFIIFLFI ″ *0701 50 ″ ″ ″ 246 260 YRWMCLRRFIIFLFI ″ *1501 23 ″ ″ ″ 246 260 YRWMCLRRFIIFLFI ″ *1101 75 ″ ″ ″ 247 261 RWMCLRRFIIFLFIL 1419 *1301 95 ″ ″ ″ 247 261 RWMCLRRFIIFLFIL ″ *0701 30 ″ ″ ″ 247 261 RWMCLRRFIIFLFIL ″ *1501 10 ″ ″ ″ 247 261 RWMCLRRFIIFLFIL ″ *1101 45 ″ ″ ″ 248 262 WMCLRRFIIFLFILL 1420 *1301 93 ″ ″ ″ 248 262 WMCLRRFIIFLFILL ″ *1501 73 ″ ″ ″ 248 262 WMCLRRFIIFLFILL ″ *0701 60 ″ ″ ″ 248 262 WMCLRRFIIFLFILL ″ *0301 28 ″ ″ ″ 249 263 MCLRRFIIFLFILLL 1421 *1501 95 ″ ″ ″ 249 263 MCLRRFIIFLFILLL ″ *1301 90 ″ ″ ″ 249 263 MCLRRFIIFLFILLL ″ *0301 80 ″ ″ ″ 249 263 MCLRRFIIFLFILLL ″ *0701 58 ″ ″ ″ 249 263 MCLRRFIIFLFILLL ″ *0101 53 ″ ″ ″ 249 263 MCLRRFIIFLFILLL ″ *1101 50 ″ ″ ″ 249 263 MCLRRFIIFLFILLL ″ *0401 3 ″ ″ ″ 250 264 CLRRFIIFLFILLLC 1422 *1301 88 ″ ″ ″ 250 264 CLRRFIIFLFILLLC ″ *0301 78 ″ ″ ″ 250 264 CLRRFIIFLFILLLC ″ *1501 68 ″ ″ ″ 250 264 CLRRFIIFLFILLLC ″ *0701 55 ″ ″ ″ 250 264 CLRRFIIFLFILLLC ″ *0101 48 ″ ″ ″ 250 264 CLRRFIIFLFILLLC ″ *1101 48 ″ ″ ″ 251 265 LRRFIIFLFILLLCL 1423 *1501 100 ″ ″ ″ 251 265 LRRFIIFLFILLLCL ″ *1301 85 ″ ″ ″ 251 265 LRRFIIFLFILLLCL ″ *0101 83 ″ ″ ″ 251 265 LRRFIIFLFILLLCL ″ *0301 83 ″ ″ ″ 251 265 LRRFIIFLFILLLCL ″ *1101 58 ″ ″ ″ 251 265 LRRFIIFLFILLLCL ″ *0701 53 ″ ″ ″ 252 266 RRFIIFLFILLLCLI 1424 *1501 98 ″ ″ ″ 252 266 RRFIIFLFILLLCLI ″ *0101 80 ″ ″ ″ 252 266 RRFIIFLFILLLCLI ″ *1101 55 ″ ″ ″ 252 266 RRFIIFLFILLLCLI ″ *0301 40 ″ ″ ″ 252 266 RRFIIFLFILLLCLI ″ *0701 38 ″ ″ ″ 252 266 RRFIIFLFILLLCLI ″ *1301 35 ″ ″ ″ 253 267 RFIIFLFILLLCLIF 1425 *1101 100 ″ ″ ″ 253 267 RFIIFLFILLLCLIF ″ *0101 78 ″ ″ ″ 253 267 RFIIFLFILLLCLIF ″ *1501 60 ″ ″ ″ 253 267 RFIIFLFILLLCLIF ″ *0301 38 ″ ″ ″ 253 267 RFIIFLFILLLCLIF ″ *0701 35 ″ ″ ″ 253 267 RFIIFLFILLLCLIF ″ *1301 33 ″ ″ ″ 253 267 RFIIFLFILLLCLIF ″ *0401 8 ″ ″ ″ 254 268 FIIFLFILLLCLIFL 1426 *1101 98 ″ ″ ″ 254 268 FIIFLFILLLCLIFL ″ *1501 88 ″ ″ ″ 254 268 FIIFLFILLLCLIFL ″ *0101 65 ″ ″ ″ 254 268 FIIFLFILLLCLIFL ″ *0301 35 ″ ″ ″ 254 268 FIIFLFILLLCLIFL ″ *1301 30 ″ ″ ″ 254 268 FIIFLFILLLCLIFL ″ *0401 13 ″ ″ ″ 255 269 IIFLFILLLCLIFLL 1427 *1101 95 ″ ″ ″ 255 269 IIFLFILLLCLIFLL ″ *1501 93 ″ ″ ″ 255 269 IIFLFILLLCLIFLL ″ *0301 70 ″ ″ ″ 255 269 IIFLFILLLCLIFLL ″ *0101 35 ″ ″ ″ 255 269 IIFLFILLLCLIFLL ″ *0401 35 ″ ″ ″ 255 269 IIFLFILLLCLIFLL ″ *1301 28 ″ ″ ″ 256 270 IFLFILLLCLIFLLV 1428 *1101 93 ″ ″ ″ 256 270 IFLFILLLCLIFLLV ″ *0301 68 ″ ″ ″ 256 270 IFLFILLLCLIFLLV ″ *1501 53 ″ ″ ″ 256 270 IFLFILLLCLIFLLV ″ *0101 30 ″ ″ ″ 256 270 IFLFILLLCLIFLLV ″ *1301 25 ″ ″ ″ 256 270 IFLFILLLCLIFLLV ″ *0401 10 ″ ″ ″ 257 271 FLFILLLCLIFLLVL 1429 *1101 90 ″ ″ ″ 257 271 FLFILLLCLIFLLVL ″ *0301 65 ″ ″ ″ 257 271 FLFILLLCLIFLLVL ″ *1501 58 ″ ″ ″ 257 271 FLFILLLCLIFLLVL ″ *0101 28 ″ ″ ″ 257 271 FLFILLLCLIFLLVL ″ *1301 23 ″ ″ ″ 257 271 FLFILLLCLIFLLVL ″ *0401 18 ″ ″ ″ 258 272 LFILLLCLIFLLVLL 1430 *1101 88 ″ ″ ″ 258 272 LFILLLCLIFLLVLL ″ *0301 63 ″ ″ ″ 258 272 LFILLLCLIFLLVLL ″ *1501 50 ″ ″ ″ 258 272 LFILLLCLIFLLVLL ″ *0101 25 ″ ″ ″ 258 272 LFILLLCLIFLLVLL ″ *1301 20 ″ ″ ″ 259 273 FILLLCLIFLLVLLD 1431 *1101 85 ″ ″ ″ 259 273 FILLLCLIFLLVLLD ″ *0301 55 ″ ″ ″ 259 273 FILLLCLIFLLVLLD ″ *1501 30 ″ ″ ″ 259 273 FILLLCLIFLLVLLD ″ *0101 23 ″ ″ ″ 259 273 FILLLCLIFLLVLLD ″ *1301 18 ″ ″ ″ 260 274 ILLLCLIFLLVLLDY 1432 *1101 45 ″ ″ ″ 260 274 ILLLCLIFLLVLLDY ″ *1301 15 ″ ″ ″ 260 274 ILLLCLIFLLVLLDY ″ *1501 13 ″ ″ ″ Cumulative Class II-B score:  7238 330 344 WAFAKYLWEWASVRF 1433 *1501 5 32 323 358 331 345 AFAKYLWEWASVRFS 1434 *0401 65 ″ ″ ″ 331 345 AFAKYLWEWASVRFS ″ *0301 30 ″ ″ ″ 331 345 AFAKYLWEWASVRFS ″ *1501 15 ″ ″ ″ 331 345 AFAKYLWEWASVRFS ″ *1101 5 ″ ″ ″ 332 346 FAKYLWEWASVRFSW 1435 *0401 80 ″ ″ ″ 332 346 FAKYLWEWASVRFSW ″ *0301 55 ″ ″ ″ 332 346 FAKYLWEWASVRFSW ″ *1501 50 ″ ″ ″ 332 346 FAKYLWEWASVRFSW ″ *1101 40 ″ ″ ″ 332 346 FAKYLWEWASVRFSW ″ *0104 25 ″ ″ ″ 332 346 FAKYLWEWASVRFSW ″ *0101 23 ″ ″ ″ 332 346 FAKYLWEWASVRFSW ″ *0105 23 ″ ″ ″ 332 346 FAKYLWEWASVRFSW ″ *0107 23 ″ ″ ″ 332 346 FAKYLWEWASVRFSW ″ *0701 15 ″ ″ ″ 333 347 AKYLWEWASVRFSWL 1436 *0701 28 ″ ″ ″ 333 347 AKYLWEWASVRFSWL ″ *0401 60 ″ ″ ″ 333 347 AKYLWEWASVRFSWL ″ *0301 25 ″ ″ ″ 333 347 AKYLWEWASVRFSWL ″ *1101 25 ″ ″ ″ 333 347 AKYLWEWASVRFSWL ″ *0101 3 ″ ″ ″ 333 347 AKYLWEWASVRFSWL ″ *0105 3 ″ ″ ″ 333 347 AKYLWEWASVRFSWL ″ *0107 3 ″ ″ ″ 334 348 KYLWEWASVRFSWLS 1437 *0701 25 ″ ″ ″ 334 348 KYLWEWASVRFSWLS ″ *0401 5 ″ ″ ″ 336 350 LWEWASVRFSWLSLL 1438 *0301 33 ″ ″ ″ 337 351 WEWASVRFSWLSLLV 1439 *0301 73 ″ ″ ″ 337 351 WEWASVRFSWLSLLV ″ *1501 45 ″ ″ ″ 337 351 WEWASVRFSWLSLLV ″ *1301 25 ″ ″ ″ 338 352 EWASVRFSWLSLLVP 1440 *0301 30 ″ ″ ″ 338 352 EWASVRFSWLSLLVP ″ *1501 40 ″ ″ ″ 338 352 EWASVRFSWLSLLVP ″ *1301 35 ″ ″ ″ 339 353 WASVRFSWLSLLVPF 1441 *0301 58 ″ ″ ″ 339 353 WASVRFSWLSLLVPF ″ *1501 55 ″ ″ ″ 339 353 WASVRFSWLSLLVPF ″ *1301 50 ″ ″ ″ 339 353 WASVRFSWLSLLVPF ″ *0104 38 ″ ″ ″ 339 353 WASVRFSWLSLLVPF ″ *0102 5 ″ ″ ″ 340 354 ASVRFSWLSLLVPFV 1442 *0301 75 ″ ″ ″ 340 354 ASVRFSWLSLLVPFV ″ *0401 33 ″ ″ ″ 340 354 ASVRFSWLSLLVPFV ″ *1101 18 ″ ″ ″ 340 354 ASVRFSWLSLLVPFV ″ *0104 53 ″ ″ ″ 340 354 ASVRFSWLSLLVPFV ″ *1501 30 ″ ″ ″ 340 354 ASVRFSWLSLLVPFV ″ *0102 28 ″ ″ ″ 340 354 ASVRFSWLSLLVPFV ″ *1301 20 ″ ″ ″ 340 354 ASVRFSWLSLLVPFV ″ *0106 10 ″ ″ ″ 341 355 SVRFSWLSLLVPFVQ 1443 *0401 30 ″ ″ ″ 341 355 SVRFSWLSLLVPFVQ ″ *1101 15 ″ ″ ″ 341 355 SVRFSWLSLLVPFVQ ″ *0104 50 ″ ″ ″ 341 355 SVRFSWLSLLVPFVQ ″ *0102 23 ″ ″ ″ 341 355 SVRFSWLSLLVPFVQ ″ *0106 5 ″ ″ ″ 342 356 VRFSWLSLLVPFVQW 1444 *0401 28 ″ ″ ″ 342 356 VRFSWLSLLVPFVQW ″ *0101 15 ″ ″ ″ 342 356 VRFSWLSLLVPFVQW ″ *1101 13 ″ ″ ″ 342 356 VRFSWLSLLVPFVQW ″ *0104 15 ″ ″ ″ 343 357 RFSWLSLLVPFVQWF 1445 *0401 25 ″ ″ ″ 343 357 RFSWLSLLVPFVQWF ″ *0101 20 ″ ″ ″ 343 357 RFSWLSLLVPFVQWF ″ *1101 10 ″ ″ ″ 344 358 FSWLSLLVPFVQWFV 1446 *1501 90 ″ ″ ″ 344 358 FSWLSLLVPFVQWFV ″ *1301 70 ″ ″ ″ 344 358 FSWLSLLVPFVQWFV ″ *0401 23 ″ ″ ″ 344 358 FSWLSLLVPFVQWFV ″ *1101 8 ″ ″ ″ Cumulative Class II-B score:  1815 330 344 WAFAKYLWEWASVRF 1433 *1501 5 33 327 358 331 345 AFAKYLWEWASVRFS 1434 *0401 65 ″ ″ ″ 331 345 AFAKYLWEWASVRFS ″ *0301 30 ″ ″ ″ 331 345 AFAKYLWEWASVRFS ″ *1501 15 ″ ″ ″ 331 345 AFAKYLWEWASVRFS ″ *1101 5 ″ ″ ″ 332 346 FAKYLWEWASVRFSW 1435 *0401 80 ″ ″ ″ 332 346 FAKYLWEWASVRFSW ″ *0301 55 ″ ″ ″ 332 346 FAKYLWEWASVRFSW ″ *1501 50 ″ ″ ″ 332 346 FAKYLWEWASVRFSW ″ *1101 40 ″ ″ ″ 332 346 FAKYLWEWASVRFSW ″ *0104 25 ″ ″ ″ 332 346 FAKYLWEWASVRFSW ″ *0101 23 ″ ″ ″ 332 346 FAKYLWEWASVRFSW ″ *0105 23 ″ ″ ″ 332 346 FAKYLWEWASVRFSW ″ *0107 23 ″ ″ ″ 332 346 FAKYLWEWASVRFSW ″ *0701 15 ″ ″ ″ 333 347 AKYLWEWASVRFSWL 1436 *0701 28 ″ ″ ″ 333 347 AKYLWEWASVRFSWL ″ *0401 60 ″ ″ ″ 333 347 AKYLWEWASVRFSWL ″ *0301 25 ″ ″ ″ 333 347 AKYLWEWASVRFSWL ″ *1101 25 ″ ″ ″ 333 347 AKYLWEWASVRFSWL ″ *0101 3 ″ ″ ″ 333 347 AKYLWEWASVRFSWL ″ *0105 3 ″ ″ ″ 333 347 AKYLWEWASVRFSWL ″ *0107 3 ″ ″ ″ 334 348 KYLWEWASVRFSWLS 1437 *0701 25 ″ ″ ″ 334 348 KYLWEWASVRFSWLS ″ *0401 5 ″ ″ ″ 336 350 LWEWASVRFSWLSLL 1438 *0301 33 ″ ″ ″ 337 351 WEWASVRFSWLSLLV 1439 *0301 73 ″ ″ ″ 337 351 WEWASVRFSWLSLLV ″ *1501 45 ″ ″ ″ 337 351 WEWASVRFSWLSLLV ″ *1301 25 ″ ″ ″ 338 352 EWASVRFSWLSLLVP 1440 *0301 30 ″ ″ ″ 338 352 EWASVRFSWLSLLVP ″ *1501 40 ″ ″ ″ 338 352 EWASVRFSWLSLLVP ″ *1301 35 ″ ″ ″ 339 353 WASVRFSWLSLLVPF 1441 *0301 58 ″ ″ ″ 339 353 WASVRFSWLSLLVPF ″ *1501 55 ″ ″ ″ 339 353 WASVRFSWLSLLVPF ″ *1301 50 ″ ″ ″ 339 353 WASVRFSWLSLLVPF ″ *0104 38 ″ ″ ″ 339 353 WASVRFSWLSLLVPF ″ *0102 5 ″ ″ ″ 340 354 ASVRFSWLSLLVPFV 1442 *0301 75 ″ ″ ″ 340 354 ASVRFSWLSLLVPFV ″ *0401 33 ″ ″ ″ 340 354 ASVRFSWLSLLVPFV ″ *1101 18 ″ ″ ″ 340 354 ASVRFSWLSLLVPFV ″ *0104 53 ″ ″ ″ 340 354 ASVRFSWLSLLVPFV ″ *1501 30 ″ ″ ″ 340 354 ASVRFSWLSLLVPFV ″ *0102 28 ″ ″ ″ 340 354 ASVRFSWLSLLVPFV ″ *1301 20 ″ ″ ″ 340 354 ASVRFSWLSLLVPFV ″ *0106 10 ″ ″ ″ 341 355 SVRFSWLSLLVPFVQ 1443 *0401 30 ″ ″ ″ 341 355 SVRFSWLSLLVPFVQ ″ *1101 15 ″ ″ ″ 341 355 SVRFSWLSLLVPFVQ ″ *0104 50 ″ ″ ″ 341 355 SVRFSWLSLLVPFVQ ″ *0102 23 ″ ″ ″ 341 355 SVRFSWLSLLVPFVQ ″ *0106 5 ″ ″ ″ 342 356 VRFSWLSLLVPFVQW 1444 *0401 28 ″ ″ ″ 342 356 VRFSWLSLLVPFVQW ″ *0101 15 ″ ″ ″ 342 356 VRFSWLSLLVPFVQW ″ *1101 13 ″ ″ ″ 342 356 VRFSWLSLLVPFVQW ″ *0104 15 ″ ″ ″ 343 357 RFSWLSLLVPFVQWF 1445 *0401 25 ″ ″ ″ 343 357 RFSWLSLLVPFVQWF ″ *0101 20 ″ ″ ″ 343 357 RFSWLSLLVPFVQWF ″ *1101 10 ″ ″ ″ 344 358 FSWLSLLVPFVQWFV 1446 *1501 90 ″ ″ ″ 344 358 FSWLSLLVPFVQWFV ″ *1301 70 ″ ″ ″ 344 358 FSWLSLLVPFVQWFV ″ *0401 23 ″ ″ ″ 344 358 FSWLSLLVPFVQWFV ″ *1101 8 ″ ″ ″ Cumulative Class II-B score:  1815 330 344 WAFAKYLWEWASVRF 1433 *1501 5 34 328 358 331 345 AFAKYLWEWASVRFS 1434 *0401 65 ″ ″ ″ 331 345 AFAKYLWEWASVRFS ″ *0301 30 ″ ″ ″ 331 345 AFAKYLWEWASVRFS ″ *1501 15 ″ ″ ″ 331 345 AFAKYLWEWASVRFS ″ *1101 5 ″ ″ ″ 332 346 FAKYLWEWASVRFSW 1435 *0401 80 ″ ″ ″ 332 346 FAKYLWEWASVRFSW ″ *0301 55 ″ ″ ″ 332 346 FAKYLWEWASVRFSW ″ *1501 50 ″ ″ ″ 332 346 FAKYLWEWASVRFSW ″ *1101 40 ″ ″ ″ 332 346 FAKYLWEWASVRFSW ″ *0104 25 ″ ″ ″ 332 346 FAKYLWEWASVRFSW ″ *0101 23 ″ ″ ″ 332 346 FAKYLWEWASVRFSW ″ *0105 23 ″ ″ ″ 332 346 FAKYLWEWASVRFSW ″ *0107 23 ″ ″ ″ 332 346 FAKYLWEWASVRFSW ″ *0701 15 ″ ″ ″ 333 347 AKYLWEWASVRFSWL 1436 *0701 28 ″ ″ ″ 333 347 AKYLWEWASVRFSWL ″ *0401 60 ″ ″ ″ 333 347 AKYLWEWASVRFSWL ″ *0301 25 ″ ″ ″ 333 347 AKYLWEWASVRFSWL ″ *1101 25 ″ ″ ″ 333 347 AKYLWEWASVRFSWL ″ *0101 3 ″ ″ ″ 333 347 AKYLWEWASVRFSWL ″ *0105 3 ″ ″ ″ 333 347 AKYLWEWASVRFSWL ″ *0107 3 ″ ″ ″ 334 348 KYLWEWASVRFSWLS 1437 *0701 25 ″ ″ ″ 334 348 KYLWEWASVRFSWLS ″ *0401 5 ″ ″ ″ 336 350 LWEWASVRFSWLSLL 1438 *0301 33 ″ ″ ″ 337 351 WEWASVRFSWLSLLV 1439 *0301 73 ″ ″ ″ 337 351 WEWASVRFSWLSLLV ″ *1501 45 ″ ″ ″ 337 351 WEWASVRFSWLSLLV ″ *1301 25 ″ ″ ″ 338 352 EWASVRFSWLSLLVP 1440 *0301 30 ″ ″ ″ 338 352 EWASVRFSWLSLLVP ″ *1501 40 ″ ″ ″ 338 352 EWASVRFSWLSLLVP ″ *1301 35 ″ ″ ″ 339 353 WASVRFSWLSLLVPF 1441 *0301 58 ″ ″ ″ 339 353 WASVRFSWLSLLVPF ″ *1501 55 ″ ″ ″ 339 353 WASVRFSWLSLLVPF ″ *1301 50 ″ ″ ″ 339 353 WASVRFSWLSLLVPF ″ *0104 38 ″ ″ ″ 339 353 WASVRFSWLSLLVPF ″ *0102 5 ″ ″ ″ 340 354 ASVRFSWLSLLVPFV 1442 *0301 75 ″ ″ ″ 340 354 ASVRFSWLSLLVPFV ″ *0401 33 ″ ″ ″ 340 354 ASVRFSWLSLLVPFV ″ *1101 18 ″ ″ ″ 340 354 ASVRFSWLSLLVPFV ″ *0104 53 ″ ″ ″ 340 354 ASVRFSWLSLLVPFV ″ *1501 30 ″ ″ ″ 340 354 ASVRFSWLSLLVPFV ″ *0102 28 ″ ″ ″ 340 354 ASVRFSWLSLLVPFV ″ *1301 20 ″ ″ ″ 340 354 ASVRFSWLSLLVPFV ″ *0106 10 ″ ″ ″ 341 355 SVRFSWLSLLVPFVQ 1443 *0401 30 ″ ″ ″ 341 355 SVRFSWLSLLVPFVQ ″ *1101 15 ″ ″ ″ 341 355 SVRFSWLSLLVPFVQ ″ *0104 50 ″ ″ ″ 341 355 SVRFSWLSLLVPFVQ ″ *0102 23 ″ ″ ″ 341 355 SVRFSWLSLLVPFVQ ″ *0106 5 ″ ″ ″ 342 356 VRFSWLSLLVPFVQW 1444 *0401 28 ″ ″ ″ 342 356 VRFSWLSLLVPFVQW ″ *0101 15 ″ ″ ″ 342 356 VRFSWLSLLVPFVQW ″ *1101 13 ″ ″ ″ 342 356 VRFSWLSLLVPFVQW ″ *0104 15 ″ ″ ″ 343 357 RFSWLSLLVPFVQWF 1445 *0401 25 ″ ″ ″ 343 357 RFSWLSLLVPFVQWF ″ *0101 20 ″ ″ ″ 343 357 RFSWLSLLVPFVQWF ″ *1101 10 ″ ″ ″ 344 358 FSWLSLLVPFVQWFV 1446 *1501 90 ″ ″ ″ 344 358 FSWLSLLVPFVQWFV ″ *1301 70 ″ ″ ″ 344 358 FSWLSLLVPFVQWFV ″ *0401 23 ″ ″ ″ 344 358 FSWLSLLVPFVQWFV ″ *1101 8 ″ ″ ″ Cumulative Class II-B score:  1815 365 379 WLSAIWMMWYWGPSL 1447 *1501 35 35 365 400 366 380 LSAIWMMWYWGPSLY 1448 *1501 48 ″ ″ ″ 367 381 SAIWMMWYWGPSLYS 1449 *1501 40 ″ ″ ″ 368 382 AIWMMWYWGPSLYSI 1450 *1501 45 ″ ″ ″ 369 383 IWMMWYWGPSLYSIV 1451 *1501 38 ″ ″ ″ 369 383 IWMMWYWGPSLYSIV ″ *0101 20 ″ ″ ″ 369 383 IWMMWYWGPSLYSIV ″ *0105 20 ″ ″ ″ 369 383 IWMMWYWGPSLYSIV ″ *0107 20 ″ ″ ″ 370 384 WMMWYWGPSLYSIVS 1452 *1501 28 ″ ″ ″ 370 384 WMMWYWGPSLYSIVS ″ *0101 33 ″ ″ ″ 370 384 WMMWYWGPSLYSIVS ″ *0105 33 ″ ″ ″ 370 384 WMMWYWGPSLYSIVS ″ *0107 33 ″ ″ ″ 371 385 MMWYWGPSLYSIVSP 1453 *1501 8 ″ ″ ″ 373 387 WYWGPSLYSIVSPFI 1454 *0701 90 ″ ″ ″ 373 387 WYWGPSLYSIVSPFI ″ *0401 40 ″ ″ ″ 373 387 WYWGPSLYSIVSPFI ″ *0106 45 ″ ″ ″ 373 387 WYWGPSLYSIVSPFI ″ *0101 43 ″ ″ ″ 373 387 WYWGPSLYSIVSPFI ″ *0105 43 ″ ″ ″ 373 387 WYWGPSLYSIVSPFI ″ *0107 43 ″ ″ ″ 373 387 WYWGPSLYSIVSPFI ″ *0102 18 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP 1455 *0701 65 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP ″ *0101 60 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP ″ *0105 60 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP ″ *0107 60 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP ″ *0401 55 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP ″ *0106 53 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP ″ *0102 48 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP ″ *0104 43 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP ″ *1501 25 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL 1456 *0701 85 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *0401 20 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *1501 18 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *0104 88 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *0102 85 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *0101 83 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *0105 83 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *0106 83 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *0107 83 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *0103 15 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *1101 15 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL 1457 *0701 83 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *0401 43 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *1501 43 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *0101 33 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *0104 100 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *0102 98 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *0105 93 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *0107 93 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *0106 90 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *0103 50 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *1101 35 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *1301 15 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP 1458 *0701 63 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *1501 33 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *0101 10 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *0401 5 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *0104 93 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *0102 90 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *0106 85 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *0105 80 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *0107 80 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *0103 20 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *1101 20 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *1301 10 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI 1459 *0701 43 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *0104 83 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *0102 78 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *0106 73 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *0101 63 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *0105 63 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *0107 63 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *1501 35 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *0401 20 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *0103 5 ″ ″ ″ 379 393 LYSIVSPFIPLLPIF 1460 *0701 33 ″ ″ ″ 379 393 LYSIVSPFIPLLPIF ″ *0106 63 ″ ″ ″ 379 393 LYSIVSPFIPLLPIF ″ *0102 55 ″ ″ ″ 379 393 LYSIVSPFIPLLPIF ″ *0104 55 ″ ″ ″ 379 393 LYSIVSPFIPLLPIF ″ *0101 53 ″ ″ ″ 379 393 LYSIVSPFIPLLPIF ″ *0107 53 ″ ″ ″ 380 394 YSIVSPFIPLLPIFF 1461 *1101 35 ″ ″ ″ 380 394 YSIVSPFIPLLPIFF ″ *0101 8 ″ ″ ″ 380 394 YSIVSPFIPLLPIFF ″ *0104 23 ″ ″ ″ 380 394 YSIVSPFIPLLPIFF ″ *0106 18 ″ ″ ″ 380 394 YSIVSPFIPLLPIFF ″ *0105 5 ″ ″ ″ 380 394 YSIVSPFIPLLPIFF ″ *0107 5 ″ ″ ″ 381 395 SIVSPFIPLLPIFFC 1462 *1101 33 ″ ″ ″ 381 395 SIVSPFIPLLPIFFC ″ *0101 5 ″ ″ ″ 382 396 IVSPFIPLLPIFFCL 1463 *1101 30 ″ ″ ″ 382 396 IVSPFIPLLPIFFCL ″ *0101 3 ″ ″ ″ 382 396 IVSPFIPLLPIFFCL ″ *0104 18 ″ ″ ″ 382 396 IVSPFIPLLPIFFCL ″ *0105 15 ″ ″ ″ 382 396 IVSPFIPLLPIFFCL ″ *0107 15 ″ ″ ″ 382 396 IVSPFIPLLPIFFCL ″ *0102 3 ″ ″ ″ 383 397 VSPFIPLLPIFFCLW 1464 *1101 28 ″ ″ ″ 383 397 VSPFIPLLPIFFCLW ″ *0101 13 ″ ″ ″ 383 397 VSPFIPLLPIFFCLW ″ *0105 13 ″ ″ ″ 383 397 VSPFIPLLPIFFCLW ″ *0107 13 ″ ″ ″ 383 397 VSPFIPLLPIFFCLW ″ *0104 10 ″ ″ ″ 384 398 SPFIPLLPIFFCLWV 1465 *1101 25 ″ ″ ″ 384 398 SPFIPLLPIFFCLWV ″ *1501 5 ″ ″ ″ 386 400 FIPLLPIFFCLWVYI 1466 *1101 23 ″ ″ ″ Cumulative Class II-B score:  4425 371 385 NNWYWGPSLYSIVSP 1453 *1501 8 36 371 400 373 387 WYWGPSLYSIVSPFI 1454 *0701 90 ″ ″ ″ 373 387 WYWGPSLYSIVSPFI ″ *0401 40 ″ ″ ″ 373 387 WYWGPSLYSIVSPFI ″ *0106 45 ″ ″ ″ 373 387 WYWGPSLYSIVSPFI ″ *0101 43 ″ ″ ″ 373 387 WYWGPSLYSIVSPFI ″ *0105 43 ″ ″ ″ 373 387 WYWGPSLYSIVSPFI ″ *0107 43 ″ ″ ″ 373 387 WYWGPSLYSIVSPFI ″ *0102 18 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP 1455 *0701 65 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP ″ *0101 60 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP ″ *0105 60 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP ″ *0107 60 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP ″ *0401 55 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP ″ *0106 53 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP ″ *0102 48 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP ″ *0104 43 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP ″ *1501 25 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL 1456 *0701 85 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *0401 20 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *1501 18 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *0104 88 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *0102 85 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *0101 83 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *0105 83 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *0106 83 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *0107 83 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *0103 15 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *1101 15 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL 1457 *0701 83 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *0401 43 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *1501 43 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *0101 33 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *0104 100 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *0102 98 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *0105 93 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *0107 93 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *0106 90 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *0103 50 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *1101 35 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *1301 15 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP 1458 *0701 63 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *1501 33 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *0101 10 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *0401 5 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *0104 93 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *0102 90 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *0106 85 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *0105 80 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *0107 80 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *0103 20 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *1101 20 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *1301 10 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI 1459 *0701 43 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *0104 83 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *0102 78 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *0106 73 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *0101 63 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *0105 63 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *0107 63 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *1501 35 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *0401 20 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *0103 5 ″ ″ ″ 379 393 LYSIVSPFIPLLPIF 1460 *0701 33 ″ ″ ″ 379 393 LYSIVSPFIPLLPIF ″ *0106 63 ″ ″ ″ 379 393 LYSIVSPFIPLLPIF ″ *0102 55 ″ ″ ″ 379 393 LYSIVSPFIPLLPIF ″ *0104 55 ″ ″ ″ 379 393 LYSIVSPFIPLLPIF ″ *0101 53 ″ ″ ″ 379 393 LYSIVSPFIPLLPIF ″ *0105 53 ″ ″ ″ 379 393 LYSIVSPFIPLLPIF ″ *0107 53 ″ ″ ″ 380 394 YSIVSPFIPLLPIFF 1461 *1101 35 ″ ″ ″ 380 394 YSIVSPFIPLLPIFF ″ *0101 8 ″ ″ ″ 380 394 YSIVSPFIPLLPIFF ″ *0104 23 ″ ″ ″ 380 394 YSIVSPFIPLLPIFF ″ *0106 18 ″ ″ ″ 380 394 YSIVSPFIPLLPIFF ″ *0105 5 ″ ″ ″ 380 394 YSIVSPFIPLLPIFF ″ *0107 5 ″ ″ ″ 381 395 SIVSPFIPLLPIFFC 1462 *1101 33 ″ ″ ″ 381 395 SIVSPFIPLLPIFFC ″ *0101 5 ″ ″ ″ 382 396 IVSPFIPLLPIFFCL 1463 *1101 30 ″ ″ ″ 382 396 IVSPFIPLLPIFFCL ″ *0101 3 ″ ″ ″ 382 396 IVSPFIPLLPIFFCL ″ *0104 18 ″ ″ ″ 382 396 IVSPFIPLLPIFFCL ″ *0105 15 ″ ″ ″ 382 396 IVSPFIPLLPIFFCL ″ *0107 15 ″ ″ ″ 382 396 IVSPFIPLLPIFFCL ″ *0102 3 ″ ″ ″ 383 397 VSPFIPLLPIFFCLW 1464 *1101 28 ″ ″ ″ 383 397 VSPFIPLLPIFFCLW ″ *0101 13 ″ ″ ″ 383 397 VSPFIPLLPIFFCLW ″ *0105 13 ″ ″ ″ 383 397 VSPFIPLLPIFFCLW ″ *0107 13 ″ ″ ″ 383 397 VSPFIPLLPIFFCLW ″ *0104 10 ″ ″ ″ 384 398 SPFIPLLPIFFCLWV 1465 *1101 25 ″ ″ ″ 384 398 SPFIPLLPIFFCLWV ″ *1501 5 ″ ″ ″ 386 400 FIPLLPIFFCLWVYI 1466 *1101 23 ″ ″ ″ Cumulative Class II-B score:  4035 370 384 WMMWYWGPSLYSIVS 1452 *1501 28 37 370 400 370 384 WMMWYWGPSLYSIVS ″ *0101 33 ″ ″ ″ 370 384 WMMWYWGPSLYSIVS ″ *0105 33 ″ ″ ″ 370 384 WMMWYWGPSLYSIVS ″ *0107 33 ″ ″ ″ 371 385 MMWYWGPSLYSIVSP 1453 *1501 8 ″ ″ ″ 373 387 WYWGPSLYSIVSPFI 1454 *0701 90 ″ ″ ″ 373 387 WYWGPSLYSIVSPFI ″ *0401 40 ″ ″ ″ 373 387 WYWGPSLYSIVSPFI ″ *0106 45 ″ ″ ″ 373 387 WYWGPSLYSIVSPFI ″ *0101 43 ″ ″ ″ 373 387 WYWGPSLYSIVSPFI ″ *0105 43 ″ ″ ″ 373 387 WYWGPSLYSIVSPFI ″ *0107 43 ″ ″ ″ 373 387 WYWGPSLYSIVSPFI ″ *0102 18 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP 1455 *0701 65 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP ″ *0101 60 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP ″ *0105 60 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP ″ *0107 60 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP ″ *0401 55 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP ″ *0106 53 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP ″ *0102 48 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP ″ *0104 43 ″ ″ ″ 374 388 YWGPSLYSIVSPFIP ″ *1501 25 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL 1456 *0701 85 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *0401 20 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *1501 18 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *0104 88 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *0102 85 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *0101 83 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *0105 83 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *0106 83 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *0107 83 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *0103 15 ″ ″ ″ 375 389 WGPSLYSIVSPFIPL ″ *1101 15 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL 1457 *0701 83 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *0401 43 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *1501 43 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *0101 33 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *0104 100 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *0102 98 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *0105 93 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *0107 93 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *0106 90 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *0103 50 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *1101 35 ″ ″ ″ 376 390 GPSLYSIVSPFIPLL ″ *1301 15 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP 1458 *0701 63 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *1501 33 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *0101 10 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *0401 5 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *0104 93 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *0102 90 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *0106 85 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *0105 80 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *0107 80 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *0103 20 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *1101 20 ″ ″ ″ 377 391 PSLYSIVSPFIPLLP ″ *1301 10 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI 1459 *0701 43 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *0104 83 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *0102 78 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *0106 73 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *0101 63 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *0105 63 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *0107 63 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *1501 35 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *0401 20 ″ ″ ″ 378 392 SLYSIVSPFIPLLPI ″ *0103 5 ″ ″ ″ 379 393 LYSIVSPFIPLLPIF 1460 *0701 33 ″ ″ ″ 379 393 LYSIVSPFIPLLPIF ″ *0106 63 ″ ″ ″ 379 393 LYSIVSPFIPLLPIF ″ *0102 55 ″ ″ ″ 379 393 LYSIVSPFIPLLPIF ″ *0104 55 ″ ″ ″ 379 393 LYSIVSPFIPLLPIF ″ *0101 53 ″ ″ ″ 379 393 LYSIVSPFIPLLPIF ″ *0105 53 ″ ″ ″ 379 393 LYSIVSPFIPLLPIF ″ *0107 53 ″ ″ ″ 380 394 YSIVSPFIPLLPIFF 1461 *1101 35 ″ ″ ″ 380 394 YSIVSPFIPLLPIFF ″ *0101 8 ″ ″ ″ 380 394 YSIVSPFIPLLPIFF ″ *0104 23 ″ ″ ″ 380 394 YSIVSPFIPLLPIFF ″ *0106 18 ″ ″ ″ 380 394 YSIVSPFIPLLPIFF ″ *0105 5 ″ ″ ″ 380 394 YSIVSPFIPLLPIFF ″ *0107 5 ″ ″ ″ 381 395 SIVSPFIPLLPIFFC 1462 *1101 33 ″ ″ ″ 381 395 SIVSPFIPLLPIFFC ″ *0101 5 ″ ″ ″ 382 396 IVSPFIPLLPIFFCL 1463 *1101 30 ″ ″ ″ 382 396 IVSPFIPLLPIFFCL ″ *0101 3 ″ ″ ″ 382 396 IVSPFIPLLPIFFCL ″ *0104 18 ″ ″ ″ 382 396 IVSPFIPLLPIFFCL ″ *0105 15 ″ ″ ″ 382 396 IVSPFIPLLPIFFCL ″ *0107 15 ″ ″ ″ 382 396 IVSPFIPLLPIFFCL ″ *0102 3 ″ ″ ″ 383 397 VSPFIPLLPIFFCLW 1464 *1101 28 ″ ″ ″ 383 397 VSPFIPLLPIFFCLW ″ *0101 13 ″ ″ ″ 383 397 VSPFIPLLPIFFCLW ″ *0105 13 ″ ″ ″ 383 397 VSPFIPLLPIFFCLW ″ *0107 13 ″ ″ ″ 383 397 VSPFIPLLPIFFCLW ″ *0104 10 ″ ″ ″ 384 398 SPFIPLLPIFFCLWV 1465 *1101 25 ″ ″ ″ 384 398 SPFIPLLPIFFCLWV ″ *1501 5 ″ ″ ″ 386 400 FIPLLPIFFCLWVYI 1466 *1101 23 ″ ″ ″ 4160 Cumulative Class II-B score:  ″Start″ and ″End″ are relative to the amino acid sequence of human HBV large surface protein as depicted in SEQ ID NO: 1141 ^(A)Peptide amino acid sequence. Each HLA-DRB1 binding peptide of HBV large surface protein is listed separately for each HLA class II molecule to which it is predicted to bind, and each peptide can be listed multiple times for that reason. ^(B)B-score. See Material and Methods (Examples section). ^(C)Cumulative B-score. See Material and Methods (Examples section).

REFERENCE LIST

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The invention claimed is:
 1. An immunogenic pharmaceutical composition comprising: (a) a peptide of at least 30 and at most 40 amino acids in length and comprising an amino acid sequence selected from the group consisting of SEQ ID NOS: 51-79, 1142-1145 and 1468-1471, (b) an immune-stimulating amount of at least one pharmaceutically acceptable adjuvant selected from the group consisting of a human toll-like receptor ligand and/or agonist, Montanide ISA-51, Montanide ISA-720, dsRNA, cyclic dinucleotides (CDNs), Muramyl dipeptide (MDP), a tetanus toxin derived peptide, Interferon alpha (INFα), and combinations thereof.
 2. The composition according to claim 1, further comprising an additional peptide.
 3. The composition according to claim 1, wherein the peptide comprises an amino acid sequence of any of the proteins selected from the group consisting of HBV polymerase, HBV core protein, HBV X-protein and HBV large surface protein.
 4. The composition according to claim 1, wherein the peptide comprises an amino acid sequence selected from the group consisting of SEQ ID NOS: 51-53, 55, 57, 60, 63, 64, 66, 68, 71, 72, 74-78, 1142, 1145, 1468-1471.
 5. The composition according to claim 1, wherein the peptide comprises an amino acid sequence selected from the group consisting of SEQ ID NOS: 55, 60, 63, 64, 68, 71, 75, 77, 1142 and
 1469. 6. The composition according to claim 1, wherein the peptide further comprises a covalently linked functional group, an oligonucleotide conjugate, a sugar chain or glycan, or combinations thereof.
 7. The composition according to claim 6, wherein the covalently linked functional group is a fluorinated group.
 8. An immunogenic pharmaceutical composition comprising: (a) a polynucleotide encoding a peptide at least 30 and at most 40 amino acids in length, wherein the peptide comprises an amino acid sequence selected from the group consisting of SEQ ID NOS: 51-79, 1142-1145 and 1468-1471; (b) an immune-stimulating amount of at least one pharmaceutically acceptable adjuvant selected from the group consisting of a human toll-like receptor ligand and/or agonist, Montanide ISA-51, Montanide ISA-720, dsRNA, cyclic dinucleotides (CDNs), Muramyl dipeptide (MDP), a tetanus toxin derived peptide, Interferon alpha (IFNα), and combinations thereof.
 9. The composition according to claim 8, further comprising the peptide.
 10. The composition according to claim 8, wherein the peptide comprises an amino acid sequence of any of the proteins selected from the group consisting of HBV polymerase, HBV core protein, HBV X-protein and HBV large surface protein.
 11. The composition according to claim 8, wherein the peptide comprises an amino acid sequence selected from the group consisting of SEQ ID NOS: 51-53, 55, 57, 60, 63, 64, 66, 68, 71, 72, 74-78, 1142, 1145, and 1468-1471.
 12. The composition according to claim 8, wherein the peptide comprises an amino acid sequence selected from the group consisting of SEQ ID NOS: 55, 60, 63, 64, 68, 71, 75, 77, 1142 and
 1469. 13. The composition according to claim 9, wherein the peptide of the composition further comprises a covalently linked functional group, an oligonucleotide conjugate, a sugar chain or glycan, or combinations thereof.
 14. The composition according to claim 13, wherein the covalently linked functional group is a fluorinated group.
 15. The composition according to claim 1, further comprising PSA, 2-aminoisobutyric acid (Abu), a DC pulse cassette, or combinations thereof.
 16. The composition according to claim 1, wherein the human toll-like receptor ligand and/or agonist is selected from the group consisting of Gram positive bacterial glycolipid, LPS, LPA, LTA, fimbriae, an outer membrane protein, a heat shock protein, Mycobacterial lipoarabinomannans, dsRNA, poly(I:C), Gram negative bacterial glycolipid, a viral coat protein, a viral envelope protein, taxol and/or derivative thereof, hyaluronan containing oligosaccharides and fibronectins, bacterial flagellae, flagellin, Mycobacterial lipoproteins, group B Streptococcus heat labile soluble factor, a Staphylococcus modulin, imidazoquinolines, imiquimod and/or derivative thereof, resiquimod and/or derivative thereof, unmethylated CpG DNA, chromatin-IgG complexes, IC31, IMSAVAC, pam3cys and/or derivative thereof, poly-ICLC, and CpG oligodeoxynucleotides (CpG-ODNs).
 17. The composition according to claim 8, further comprising PSA, 2-aminoisobutyric acid (Abu), a DC pulse cassette, or combinations thereof.
 18. The composition according to claim 8, wherein the human toll-like receptor ligand and/or agonist is selected from the group consisting of Gram positive bacterial glycolipid, LPS, LPA, LTA, fimbriae, an outer membrane protein, a heat shock protein, Mycobacterial lipoarabinomannans, dsRNA, poly(I:C), Gram negative bacterial glycolipid, a viral coat protein, a viral envelope protein, taxol and/or derivative thereof, hyaluronan containing oligosaccharides and fibronectins, bacterial flagellae, flagellin, Mycobacterial lipoproteins, group B Streptococcus heat labile soluble factor, a Staphylococcus modulin, imidazoquinolines, imiquimod and/or derivative thereof, resiquimod and/or derivative thereof, unmethylated CpG DNA, chromatin-IgG complexes, IC31, IMSAVAC, pam3cys and/or derivative thereof, poly-ICLC, and CpG oligodeoxynucleotides (CpG-ODNs).
 19. The composition according to claim 1, wherein the pharmaceutically acceptable adjuvant is Montanide ISA-51.
 20. The composition according to claim 8, wherein the pharmaceutically acceptable adjuvant is Montanide ISA-51.
 21. An immunogenic pharmaceutical composition comprising a peptide of at least 30 and at most 40 amino acids in length and comprising an amino acid sequence selected from the group consisting of SEQ ID NOS: 51-79, 1142-1145 and 1468-1471, wherein the peptide further comprises a covalently linked functional group, an oligonucleotide conjugate, a sugar chain or glycan, or combinations thereof.
 22. The composition according to claim 21, wherein the covalently linked functional group is a fluorinated group.
 23. The composition according to claim 21, further comprising an immune-stimulating amount of at least one pharmaceutically acceptable adjuvant.
 24. The composition according to claim 16, wherein the pam3cys and/or derivative thereof comprises a pam3cys lipopeptide or derivative thereof.
 25. The composition according to claim 18, wherein the pam3cys and/or derivative thereof comprises a pam3cys lipopeptide or derivative thereof. 